Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex
Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Jeong, Hanbin [verfasserIn] Park, Jumi [verfasserIn] Lee, Changwook [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016 |
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| Schlagwörter: |
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| Anmerkung: |
© The Authors 2016 |
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| Übergeordnetes Werk: |
Enthalten in: EMBO Reports - Nature Publishing Group UK, 2023, 17(2016), 12 vom: 07. Nov., Seite 1857-1871 |
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| Übergeordnetes Werk: |
volume:17 ; year:2016 ; number:12 ; day:07 ; month:11 ; pages:1857-1871 |
| Links: |
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| DOI / URN: |
10.15252/embr.201642706 |
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| Katalog-ID: |
SPR05790412X |
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| 100 | 1 | |a Jeong, Hanbin |e verfasserin |0 (orcid)0000-0002-3878-1813 |4 aut | |
| 245 | 1 | 0 | |a Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex |
| 264 | 1 | |c 2016 | |
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| 337 | |a Computermedien |b c |2 rdamedia | ||
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| 520 | |a Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1‐strand comprising residues 1–7. Biochemical experiments reveal a phospholipid‐binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full‐length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74–114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head‐to‐head contact, and with Mmm1 through tail‐to‐tail contact of SMP domains. | ||
| 520 | |a Synopsis The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. The crystal structure of Mdm12 reveals a highly conserved β1‐strand that is critical for oligomerization.The SMP domain of Mdm12 selectively binds phospholipids with a positively charged head group via a negatively charged surface platform.Biochemical analysis suggests that Mdm12 provides two distinct contact sites to connect Mmm1 and Mdm34. | ||
| 520 | |a Graphical Abstract The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. | ||
| 650 | 4 | |a crystal structure |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a ERMES complex |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Mdm12 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a phospholipid binding |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a SMP domain |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Park, Jumi |e verfasserin |4 aut | |
| 700 | 1 | |a Lee, Changwook |e verfasserin |0 (orcid)0000-0002-3016-9478 |4 aut | |
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| 912 | |a GBV_ILN_22 | ||
| 912 | |a GBV_ILN_23 | ||
| 912 | |a GBV_ILN_24 | ||
| 912 | |a GBV_ILN_31 | ||
| 912 | |a GBV_ILN_32 | ||
| 912 | |a GBV_ILN_39 | ||
| 912 | |a GBV_ILN_40 | ||
| 912 | |a GBV_ILN_60 | ||
| 912 | |a GBV_ILN_62 | ||
| 912 | |a GBV_ILN_63 | ||
| 912 | |a GBV_ILN_65 | ||
| 912 | |a GBV_ILN_69 | ||
| 912 | |a GBV_ILN_70 | ||
| 912 | |a GBV_ILN_72 | ||
| 912 | |a GBV_ILN_73 | ||
| 912 | |a GBV_ILN_74 | ||
| 912 | |a GBV_ILN_90 | ||
| 912 | |a GBV_ILN_95 | ||
| 912 | |a GBV_ILN_100 | ||
| 912 | |a GBV_ILN_101 | ||
| 912 | |a GBV_ILN_105 | ||
| 912 | |a GBV_ILN_110 | ||
| 912 | |a GBV_ILN_120 | ||
| 912 | |a GBV_ILN_138 | ||
| 912 | |a GBV_ILN_150 | ||
| 912 | |a GBV_ILN_151 | ||
| 912 | |a GBV_ILN_161 | ||
| 912 | |a GBV_ILN_168 | ||
| 912 | |a GBV_ILN_170 | ||
| 912 | |a GBV_ILN_171 | ||
| 912 | |a GBV_ILN_187 | ||
| 912 | |a GBV_ILN_211 | ||
| 912 | |a GBV_ILN_213 | ||
| 912 | |a GBV_ILN_224 | ||
| 912 | |a GBV_ILN_230 | ||
| 912 | |a GBV_ILN_252 | ||
| 912 | |a GBV_ILN_266 | ||
| 912 | |a GBV_ILN_285 | ||
| 912 | |a GBV_ILN_293 | ||
| 912 | |a GBV_ILN_370 | ||
| 912 | |a GBV_ILN_602 | ||
| 912 | |a GBV_ILN_636 | ||
| 912 | |a GBV_ILN_702 | ||
| 912 | |a GBV_ILN_2001 | ||
| 912 | |a GBV_ILN_2003 | ||
| 912 | |a GBV_ILN_2004 | ||
| 912 | |a GBV_ILN_2005 | ||
| 912 | |a GBV_ILN_2006 | ||
| 912 | |a GBV_ILN_2007 | ||
| 912 | |a GBV_ILN_2008 | ||
| 912 | |a GBV_ILN_2009 | ||
| 912 | |a GBV_ILN_2010 | ||
| 912 | |a GBV_ILN_2011 | ||
| 912 | |a GBV_ILN_2014 | ||
| 912 | |a GBV_ILN_2015 | ||
| 912 | |a GBV_ILN_2018 | ||
| 912 | |a GBV_ILN_2020 | ||
| 912 | |a GBV_ILN_2021 | ||
| 912 | |a GBV_ILN_2025 | ||
| 912 | |a GBV_ILN_2026 | ||
| 912 | |a GBV_ILN_2027 | ||
| 912 | |a GBV_ILN_2034 | ||
| 912 | |a GBV_ILN_2037 | ||
| 912 | |a GBV_ILN_2038 | ||
| 912 | |a GBV_ILN_2044 | ||
| 912 | |a GBV_ILN_2048 | ||
| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
| 912 | |a GBV_ILN_2055 | ||
| 912 | |a GBV_ILN_2056 | ||
| 912 | |a GBV_ILN_2057 | ||
| 912 | |a GBV_ILN_2059 | ||
| 912 | |a GBV_ILN_2061 | ||
| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2068 | ||
| 912 | |a GBV_ILN_2088 | ||
| 912 | |a GBV_ILN_2093 | ||
| 912 | |a GBV_ILN_2106 | ||
| 912 | |a GBV_ILN_2108 | ||
| 912 | |a GBV_ILN_2110 | ||
| 912 | |a GBV_ILN_2111 | ||
| 912 | |a GBV_ILN_2113 | ||
| 912 | |a GBV_ILN_2118 | ||
| 912 | |a GBV_ILN_2119 | ||
| 912 | |a GBV_ILN_2122 | ||
| 912 | |a GBV_ILN_2129 | ||
| 912 | |a GBV_ILN_2143 | ||
| 912 | |a GBV_ILN_2144 | ||
| 912 | |a GBV_ILN_2147 | ||
| 912 | |a GBV_ILN_2148 | ||
| 912 | |a GBV_ILN_2152 | ||
| 912 | |a GBV_ILN_2153 | ||
| 912 | |a GBV_ILN_2188 | ||
| 912 | |a GBV_ILN_2190 | ||
| 912 | |a GBV_ILN_2232 | ||
| 912 | |a GBV_ILN_2336 | ||
| 912 | |a GBV_ILN_2470 | ||
| 912 | |a GBV_ILN_2472 | ||
| 912 | |a GBV_ILN_2507 | ||
| 912 | |a GBV_ILN_2522 | ||
| 912 | |a GBV_ILN_2548 | ||
| 912 | |a GBV_ILN_4012 | ||
| 912 | |a GBV_ILN_4029 | ||
| 912 | |a GBV_ILN_4035 | ||
| 912 | |a GBV_ILN_4037 | ||
| 912 | |a GBV_ILN_4046 | ||
| 912 | |a GBV_ILN_4112 | ||
| 912 | |a GBV_ILN_4125 | ||
| 912 | |a GBV_ILN_4126 | ||
| 912 | |a GBV_ILN_4155 | ||
| 912 | |a GBV_ILN_4242 | ||
| 912 | |a GBV_ILN_4246 | ||
| 912 | |a GBV_ILN_4249 | ||
| 912 | |a GBV_ILN_4251 | ||
| 912 | |a GBV_ILN_4305 | ||
| 912 | |a GBV_ILN_4306 | ||
| 912 | |a GBV_ILN_4307 | ||
| 912 | |a GBV_ILN_4313 | ||
| 912 | |a GBV_ILN_4322 | ||
| 912 | |a GBV_ILN_4323 | ||
| 912 | |a GBV_ILN_4324 | ||
| 912 | |a GBV_ILN_4325 | ||
| 912 | |a GBV_ILN_4326 | ||
| 912 | |a GBV_ILN_4328 | ||
| 912 | |a GBV_ILN_4333 | ||
| 912 | |a GBV_ILN_4334 | ||
| 912 | |a GBV_ILN_4335 | ||
| 912 | |a GBV_ILN_4336 | ||
| 912 | |a GBV_ILN_4338 | ||
| 912 | |a GBV_ILN_4367 | ||
| 912 | |a GBV_ILN_4393 | ||
| 912 | |a GBV_ILN_4700 | ||
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10.15252/embr.201642706 doi (DE-627)SPR05790412X (SPR)embr.201642706-e DE-627 ger DE-627 rakwb eng Jeong, Hanbin verfasserin (orcid)0000-0002-3878-1813 aut Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Authors 2016 Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1‐strand comprising residues 1–7. Biochemical experiments reveal a phospholipid‐binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full‐length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74–114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head‐to‐head contact, and with Mmm1 through tail‐to‐tail contact of SMP domains. Synopsis The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. The crystal structure of Mdm12 reveals a highly conserved β1‐strand that is critical for oligomerization.The SMP domain of Mdm12 selectively binds phospholipids with a positively charged head group via a negatively charged surface platform.Biochemical analysis suggests that Mdm12 provides two distinct contact sites to connect Mmm1 and Mdm34. Graphical Abstract The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. crystal structure (dpeaa)DE-He213 ERMES complex (dpeaa)DE-He213 Mdm12 (dpeaa)DE-He213 phospholipid binding (dpeaa)DE-He213 SMP domain (dpeaa)DE-He213 Park, Jumi verfasserin aut Lee, Changwook verfasserin (orcid)0000-0002-3016-9478 aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 17(2016), 12 vom: 07. Nov., Seite 1857-1871 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:17 year:2016 number:12 day:07 month:11 pages:1857-1871 https://dx.doi.org/10.15252/embr.201642706 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 17 2016 12 07 11 1857-1871 |
| spelling |
10.15252/embr.201642706 doi (DE-627)SPR05790412X (SPR)embr.201642706-e DE-627 ger DE-627 rakwb eng Jeong, Hanbin verfasserin (orcid)0000-0002-3878-1813 aut Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Authors 2016 Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1‐strand comprising residues 1–7. Biochemical experiments reveal a phospholipid‐binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full‐length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74–114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head‐to‐head contact, and with Mmm1 through tail‐to‐tail contact of SMP domains. Synopsis The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. The crystal structure of Mdm12 reveals a highly conserved β1‐strand that is critical for oligomerization.The SMP domain of Mdm12 selectively binds phospholipids with a positively charged head group via a negatively charged surface platform.Biochemical analysis suggests that Mdm12 provides two distinct contact sites to connect Mmm1 and Mdm34. Graphical Abstract The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. crystal structure (dpeaa)DE-He213 ERMES complex (dpeaa)DE-He213 Mdm12 (dpeaa)DE-He213 phospholipid binding (dpeaa)DE-He213 SMP domain (dpeaa)DE-He213 Park, Jumi verfasserin aut Lee, Changwook verfasserin (orcid)0000-0002-3016-9478 aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 17(2016), 12 vom: 07. Nov., Seite 1857-1871 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:17 year:2016 number:12 day:07 month:11 pages:1857-1871 https://dx.doi.org/10.15252/embr.201642706 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 17 2016 12 07 11 1857-1871 |
| allfields_unstemmed |
10.15252/embr.201642706 doi (DE-627)SPR05790412X (SPR)embr.201642706-e DE-627 ger DE-627 rakwb eng Jeong, Hanbin verfasserin (orcid)0000-0002-3878-1813 aut Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Authors 2016 Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1‐strand comprising residues 1–7. Biochemical experiments reveal a phospholipid‐binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full‐length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74–114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head‐to‐head contact, and with Mmm1 through tail‐to‐tail contact of SMP domains. Synopsis The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. The crystal structure of Mdm12 reveals a highly conserved β1‐strand that is critical for oligomerization.The SMP domain of Mdm12 selectively binds phospholipids with a positively charged head group via a negatively charged surface platform.Biochemical analysis suggests that Mdm12 provides two distinct contact sites to connect Mmm1 and Mdm34. Graphical Abstract The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. crystal structure (dpeaa)DE-He213 ERMES complex (dpeaa)DE-He213 Mdm12 (dpeaa)DE-He213 phospholipid binding (dpeaa)DE-He213 SMP domain (dpeaa)DE-He213 Park, Jumi verfasserin aut Lee, Changwook verfasserin (orcid)0000-0002-3016-9478 aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 17(2016), 12 vom: 07. Nov., Seite 1857-1871 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:17 year:2016 number:12 day:07 month:11 pages:1857-1871 https://dx.doi.org/10.15252/embr.201642706 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 17 2016 12 07 11 1857-1871 |
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10.15252/embr.201642706 doi (DE-627)SPR05790412X (SPR)embr.201642706-e DE-627 ger DE-627 rakwb eng Jeong, Hanbin verfasserin (orcid)0000-0002-3878-1813 aut Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Authors 2016 Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1‐strand comprising residues 1–7. Biochemical experiments reveal a phospholipid‐binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full‐length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74–114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head‐to‐head contact, and with Mmm1 through tail‐to‐tail contact of SMP domains. Synopsis The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. The crystal structure of Mdm12 reveals a highly conserved β1‐strand that is critical for oligomerization.The SMP domain of Mdm12 selectively binds phospholipids with a positively charged head group via a negatively charged surface platform.Biochemical analysis suggests that Mdm12 provides two distinct contact sites to connect Mmm1 and Mdm34. Graphical Abstract The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. crystal structure (dpeaa)DE-He213 ERMES complex (dpeaa)DE-He213 Mdm12 (dpeaa)DE-He213 phospholipid binding (dpeaa)DE-He213 SMP domain (dpeaa)DE-He213 Park, Jumi verfasserin aut Lee, Changwook verfasserin (orcid)0000-0002-3016-9478 aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 17(2016), 12 vom: 07. Nov., Seite 1857-1871 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:17 year:2016 number:12 day:07 month:11 pages:1857-1871 https://dx.doi.org/10.15252/embr.201642706 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 17 2016 12 07 11 1857-1871 |
| allfieldsSound |
10.15252/embr.201642706 doi (DE-627)SPR05790412X (SPR)embr.201642706-e DE-627 ger DE-627 rakwb eng Jeong, Hanbin verfasserin (orcid)0000-0002-3878-1813 aut Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Authors 2016 Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1‐strand comprising residues 1–7. Biochemical experiments reveal a phospholipid‐binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full‐length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74–114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head‐to‐head contact, and with Mmm1 through tail‐to‐tail contact of SMP domains. Synopsis The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. The crystal structure of Mdm12 reveals a highly conserved β1‐strand that is critical for oligomerization.The SMP domain of Mdm12 selectively binds phospholipids with a positively charged head group via a negatively charged surface platform.Biochemical analysis suggests that Mdm12 provides two distinct contact sites to connect Mmm1 and Mdm34. Graphical Abstract The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. crystal structure (dpeaa)DE-He213 ERMES complex (dpeaa)DE-He213 Mdm12 (dpeaa)DE-He213 phospholipid binding (dpeaa)DE-He213 SMP domain (dpeaa)DE-He213 Park, Jumi verfasserin aut Lee, Changwook verfasserin (orcid)0000-0002-3016-9478 aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 17(2016), 12 vom: 07. Nov., Seite 1857-1871 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:17 year:2016 number:12 day:07 month:11 pages:1857-1871 https://dx.doi.org/10.15252/embr.201642706 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 17 2016 12 07 11 1857-1871 |
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English |
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Enthalten in EMBO Reports 17(2016), 12 vom: 07. Nov., Seite 1857-1871 volume:17 year:2016 number:12 day:07 month:11 pages:1857-1871 |
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Enthalten in EMBO Reports 17(2016), 12 vom: 07. Nov., Seite 1857-1871 volume:17 year:2016 number:12 day:07 month:11 pages:1857-1871 |
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crystal structure ERMES complex Mdm12 phospholipid binding SMP domain |
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Jeong, Hanbin @@aut@@ Park, Jumi @@aut@@ Lee, Changwook @@aut@@ |
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2016-11-07T00:00:00Z |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">SPR05790412X</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20241019064926.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">241019s2016 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.15252/embr.201642706</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR05790412X</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)embr.201642706-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Jeong, Hanbin</subfield><subfield code="e">verfasserin</subfield><subfield code="0">(orcid)0000-0002-3878-1813</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2016</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© The Authors 2016</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1‐strand comprising residues 1–7. Biochemical experiments reveal a phospholipid‐binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full‐length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74–114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head‐to‐head contact, and with Mmm1 through tail‐to‐tail contact of SMP domains.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Synopsis The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. The crystal structure of Mdm12 reveals a highly conserved β1‐strand that is critical for oligomerization.The SMP domain of Mdm12 selectively binds phospholipids with a positively charged head group via a negatively charged surface platform.Biochemical analysis suggests that Mdm12 provides two distinct contact sites to connect Mmm1 and Mdm34.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Graphical Abstract The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">crystal structure</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">ERMES complex</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Mdm12</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">phospholipid binding</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">SMP domain</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Park, Jumi</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lee, Changwook</subfield><subfield code="e">verfasserin</subfield><subfield code="0">(orcid)0000-0002-3016-9478</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">EMBO Reports</subfield><subfield code="d">Nature Publishing Group UK, 2023</subfield><subfield code="g">17(2016), 12 vom: 07. 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Jeong, Hanbin |
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Jeong, Hanbin misc crystal structure misc ERMES complex misc Mdm12 misc phospholipid binding misc SMP domain Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex |
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Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex crystal structure (dpeaa)DE-He213 ERMES complex (dpeaa)DE-He213 Mdm12 (dpeaa)DE-He213 phospholipid binding (dpeaa)DE-He213 SMP domain (dpeaa)DE-He213 |
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Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex |
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Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex |
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Jeong, Hanbin |
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crystal structure of mdm12 reveals the architecture and dynamic organization of the ermes complex |
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Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex |
| abstract |
Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1‐strand comprising residues 1–7. Biochemical experiments reveal a phospholipid‐binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full‐length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74–114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head‐to‐head contact, and with Mmm1 through tail‐to‐tail contact of SMP domains. Synopsis The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. The crystal structure of Mdm12 reveals a highly conserved β1‐strand that is critical for oligomerization.The SMP domain of Mdm12 selectively binds phospholipids with a positively charged head group via a negatively charged surface platform.Biochemical analysis suggests that Mdm12 provides two distinct contact sites to connect Mmm1 and Mdm34. Graphical Abstract The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. © The Authors 2016 |
| abstractGer |
Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1‐strand comprising residues 1–7. Biochemical experiments reveal a phospholipid‐binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full‐length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74–114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head‐to‐head contact, and with Mmm1 through tail‐to‐tail contact of SMP domains. Synopsis The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. The crystal structure of Mdm12 reveals a highly conserved β1‐strand that is critical for oligomerization.The SMP domain of Mdm12 selectively binds phospholipids with a positively charged head group via a negatively charged surface platform.Biochemical analysis suggests that Mdm12 provides two distinct contact sites to connect Mmm1 and Mdm34. Graphical Abstract The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. © The Authors 2016 |
| abstract_unstemmed |
Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1‐strand comprising residues 1–7. Biochemical experiments reveal a phospholipid‐binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full‐length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74–114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head‐to‐head contact, and with Mmm1 through tail‐to‐tail contact of SMP domains. Synopsis The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. The crystal structure of Mdm12 reveals a highly conserved β1‐strand that is critical for oligomerization.The SMP domain of Mdm12 selectively binds phospholipids with a positively charged head group via a negatively charged surface platform.Biochemical analysis suggests that Mdm12 provides two distinct contact sites to connect Mmm1 and Mdm34. Graphical Abstract The crystal structure of Mdm12, a cytosolic component of the ER–mitochondria encounter structure (ERMES) complex, reveals the structural basis for phospholipid binding and selectivity of Mdm12, and the organization of SMP domains in the ERMES complex. © The Authors 2016 |
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| title_short |
Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex |
| url |
https://dx.doi.org/10.15252/embr.201642706 |
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Park, Jumi Lee, Changwook |
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| score |
7.401043 |