The crystal structure of MreC provides insights into polymer formation

MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coile...
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Autor*in:	Qin Xu [verfasserIn] Ning Sun [verfasserIn] Qingjie Xiao [verfasserIn] Chia‐ying Huang [verfasserIn] Mengxue Xu [verfasserIn] Weizhe Zhang [verfasserIn] Lina Li [verfasserIn] Qisheng Wang [verfasserIn] Vincent Olieric [verfasserIn] Weiwu Wang [verfasserIn] Jianhua He [verfasserIn] Bo Sun [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	cell shape‐determining protein crystal structure filament‐like structure MreC polymer formation

Übergeordnetes Werk:	In: FEBS Open Bio - Wiley, 2013, 12(2022), 2, Seite 340-348
Übergeordnetes Werk:	volume:12 ; year:2022 ; number:2 ; pages:340-348

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1002/2211-5463.13296

Katalog-ID:	DOAJ047649569

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245	1	4	\|a The crystal structure of MreC provides insights into polymer formation
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520			\|a MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coiled‐coil domain and two six‐stranded barrel domains. The coiled‐coil domain is essential for dimer formation, and the two monomers are prone to relative motion that is related to the small interface of β‐barrel domains. In addition, MreC forms an antiparallel filament‐like structure along the coiled‐coil direction, which is different from the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC.
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912			\|a GBV_ILN_224
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912			\|a GBV_ILN_293
912			\|a GBV_ILN_602
912			\|a GBV_ILN_636
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912			\|a GBV_ILN_2005
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912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
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912			\|a GBV_ILN_2522
912			\|a GBV_ILN_4012
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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_4242
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
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912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
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allfields	10.1002/2211-5463.13296 doi (DE-627)DOAJ047649569 (DE-599)DOAJ689707c1a13b4ccd84a6e8fcfaa1a6cf DE-627 ger DE-627 rakwb eng QH301-705.5 Qin Xu verfasserin aut The crystal structure of MreC provides insights into polymer formation 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coiled‐coil domain and two six‐stranded barrel domains. The coiled‐coil domain is essential for dimer formation, and the two monomers are prone to relative motion that is related to the small interface of β‐barrel domains. In addition, MreC forms an antiparallel filament‐like structure along the coiled‐coil direction, which is different from the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC. cell shape‐determining protein crystal structure filament‐like structure MreC polymer formation Biology (General) Ning Sun verfasserin aut Qingjie Xiao verfasserin aut Chia‐ying Huang verfasserin aut Mengxue Xu verfasserin aut Weizhe Zhang verfasserin aut Lina Li verfasserin aut Qisheng Wang verfasserin aut Vincent Olieric verfasserin aut Weiwu Wang verfasserin aut Jianhua He verfasserin aut Bo Sun verfasserin aut In FEBS Open Bio Wiley, 2013 12(2022), 2, Seite 340-348 (DE-627)686948351 (DE-600)2651702-4 22115463 nnns volume:12 year:2022 number:2 pages:340-348 https://doi.org/10.1002/2211-5463.13296 kostenfrei https://doaj.org/article/689707c1a13b4ccd84a6e8fcfaa1a6cf kostenfrei https://doi.org/10.1002/2211-5463.13296 kostenfrei https://doaj.org/toc/2211-5463 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 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_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2022 2 340-348
spelling	10.1002/2211-5463.13296 doi (DE-627)DOAJ047649569 (DE-599)DOAJ689707c1a13b4ccd84a6e8fcfaa1a6cf DE-627 ger DE-627 rakwb eng QH301-705.5 Qin Xu verfasserin aut The crystal structure of MreC provides insights into polymer formation 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coiled‐coil domain and two six‐stranded barrel domains. The coiled‐coil domain is essential for dimer formation, and the two monomers are prone to relative motion that is related to the small interface of β‐barrel domains. In addition, MreC forms an antiparallel filament‐like structure along the coiled‐coil direction, which is different from the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC. cell shape‐determining protein crystal structure filament‐like structure MreC polymer formation Biology (General) Ning Sun verfasserin aut Qingjie Xiao verfasserin aut Chia‐ying Huang verfasserin aut Mengxue Xu verfasserin aut Weizhe Zhang verfasserin aut Lina Li verfasserin aut Qisheng Wang verfasserin aut Vincent Olieric verfasserin aut Weiwu Wang verfasserin aut Jianhua He verfasserin aut Bo Sun verfasserin aut In FEBS Open Bio Wiley, 2013 12(2022), 2, Seite 340-348 (DE-627)686948351 (DE-600)2651702-4 22115463 nnns volume:12 year:2022 number:2 pages:340-348 https://doi.org/10.1002/2211-5463.13296 kostenfrei https://doaj.org/article/689707c1a13b4ccd84a6e8fcfaa1a6cf kostenfrei https://doi.org/10.1002/2211-5463.13296 kostenfrei https://doaj.org/toc/2211-5463 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 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_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2022 2 340-348
allfields_unstemmed	10.1002/2211-5463.13296 doi (DE-627)DOAJ047649569 (DE-599)DOAJ689707c1a13b4ccd84a6e8fcfaa1a6cf DE-627 ger DE-627 rakwb eng QH301-705.5 Qin Xu verfasserin aut The crystal structure of MreC provides insights into polymer formation 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coiled‐coil domain and two six‐stranded barrel domains. The coiled‐coil domain is essential for dimer formation, and the two monomers are prone to relative motion that is related to the small interface of β‐barrel domains. In addition, MreC forms an antiparallel filament‐like structure along the coiled‐coil direction, which is different from the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC. cell shape‐determining protein crystal structure filament‐like structure MreC polymer formation Biology (General) Ning Sun verfasserin aut Qingjie Xiao verfasserin aut Chia‐ying Huang verfasserin aut Mengxue Xu verfasserin aut Weizhe Zhang verfasserin aut Lina Li verfasserin aut Qisheng Wang verfasserin aut Vincent Olieric verfasserin aut Weiwu Wang verfasserin aut Jianhua He verfasserin aut Bo Sun verfasserin aut In FEBS Open Bio Wiley, 2013 12(2022), 2, Seite 340-348 (DE-627)686948351 (DE-600)2651702-4 22115463 nnns volume:12 year:2022 number:2 pages:340-348 https://doi.org/10.1002/2211-5463.13296 kostenfrei https://doaj.org/article/689707c1a13b4ccd84a6e8fcfaa1a6cf kostenfrei https://doi.org/10.1002/2211-5463.13296 kostenfrei https://doaj.org/toc/2211-5463 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 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_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2022 2 340-348
allfieldsGer	10.1002/2211-5463.13296 doi (DE-627)DOAJ047649569 (DE-599)DOAJ689707c1a13b4ccd84a6e8fcfaa1a6cf DE-627 ger DE-627 rakwb eng QH301-705.5 Qin Xu verfasserin aut The crystal structure of MreC provides insights into polymer formation 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coiled‐coil domain and two six‐stranded barrel domains. The coiled‐coil domain is essential for dimer formation, and the two monomers are prone to relative motion that is related to the small interface of β‐barrel domains. In addition, MreC forms an antiparallel filament‐like structure along the coiled‐coil direction, which is different from the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC. cell shape‐determining protein crystal structure filament‐like structure MreC polymer formation Biology (General) Ning Sun verfasserin aut Qingjie Xiao verfasserin aut Chia‐ying Huang verfasserin aut Mengxue Xu verfasserin aut Weizhe Zhang verfasserin aut Lina Li verfasserin aut Qisheng Wang verfasserin aut Vincent Olieric verfasserin aut Weiwu Wang verfasserin aut Jianhua He verfasserin aut Bo Sun verfasserin aut In FEBS Open Bio Wiley, 2013 12(2022), 2, Seite 340-348 (DE-627)686948351 (DE-600)2651702-4 22115463 nnns volume:12 year:2022 number:2 pages:340-348 https://doi.org/10.1002/2211-5463.13296 kostenfrei https://doaj.org/article/689707c1a13b4ccd84a6e8fcfaa1a6cf kostenfrei https://doi.org/10.1002/2211-5463.13296 kostenfrei https://doaj.org/toc/2211-5463 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 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_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2022 2 340-348
allfieldsSound	10.1002/2211-5463.13296 doi (DE-627)DOAJ047649569 (DE-599)DOAJ689707c1a13b4ccd84a6e8fcfaa1a6cf DE-627 ger DE-627 rakwb eng QH301-705.5 Qin Xu verfasserin aut The crystal structure of MreC provides insights into polymer formation 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coiled‐coil domain and two six‐stranded barrel domains. The coiled‐coil domain is essential for dimer formation, and the two monomers are prone to relative motion that is related to the small interface of β‐barrel domains. In addition, MreC forms an antiparallel filament‐like structure along the coiled‐coil direction, which is different from the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC. cell shape‐determining protein crystal structure filament‐like structure MreC polymer formation Biology (General) Ning Sun verfasserin aut Qingjie Xiao verfasserin aut Chia‐ying Huang verfasserin aut Mengxue Xu verfasserin aut Weizhe Zhang verfasserin aut Lina Li verfasserin aut Qisheng Wang verfasserin aut Vincent Olieric verfasserin aut Weiwu Wang verfasserin aut Jianhua He verfasserin aut Bo Sun verfasserin aut In FEBS Open Bio Wiley, 2013 12(2022), 2, Seite 340-348 (DE-627)686948351 (DE-600)2651702-4 22115463 nnns volume:12 year:2022 number:2 pages:340-348 https://doi.org/10.1002/2211-5463.13296 kostenfrei https://doaj.org/article/689707c1a13b4ccd84a6e8fcfaa1a6cf kostenfrei https://doi.org/10.1002/2211-5463.13296 kostenfrei https://doaj.org/toc/2211-5463 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 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_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2022 2 340-348
language	English
source	In FEBS Open Bio 12(2022), 2, Seite 340-348 volume:12 year:2022 number:2 pages:340-348
sourceStr	In FEBS Open Bio 12(2022), 2, Seite 340-348 volume:12 year:2022 number:2 pages:340-348
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	cell shape‐determining protein crystal structure filament‐like structure MreC polymer formation Biology (General)
isfreeaccess_bool	true
container_title	FEBS Open Bio
authorswithroles_txt_mv	Qin Xu @@aut@@ Ning Sun @@aut@@ Qingjie Xiao @@aut@@ Chia‐ying Huang @@aut@@ Mengxue Xu @@aut@@ Weizhe Zhang @@aut@@ Lina Li @@aut@@ Qisheng Wang @@aut@@ Vincent Olieric @@aut@@ Weiwu Wang @@aut@@ Jianhua He @@aut@@ Bo Sun @@aut@@
publishDateDaySort_date	2022-01-01T00:00:00Z
hierarchy_top_id	686948351
id	DOAJ047649569
language_de	englisch
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callnumber-first	Q - Science
author	Qin Xu
spellingShingle	Qin Xu misc QH301-705.5 misc cell shape‐determining protein misc crystal structure misc filament‐like structure misc MreC misc polymer formation misc Biology (General) The crystal structure of MreC provides insights into polymer formation
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topic_title	QH301-705.5 The crystal structure of MreC provides insights into polymer formation cell shape‐determining protein crystal structure filament‐like structure MreC polymer formation
topic	misc QH301-705.5 misc cell shape‐determining protein misc crystal structure misc filament‐like structure misc MreC misc polymer formation misc Biology (General)
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title	The crystal structure of MreC provides insights into polymer formation
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title_full	The crystal structure of MreC provides insights into polymer formation
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title_sort	crystal structure of mrec provides insights into polymer formation
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title_auth	The crystal structure of MreC provides insights into polymer formation
abstract	MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coiled‐coil domain and two six‐stranded barrel domains. The coiled‐coil domain is essential for dimer formation, and the two monomers are prone to relative motion that is related to the small interface of β‐barrel domains. In addition, MreC forms an antiparallel filament‐like structure along the coiled‐coil direction, which is different from the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC.
abstractGer	MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coiled‐coil domain and two six‐stranded barrel domains. The coiled‐coil domain is essential for dimer formation, and the two monomers are prone to relative motion that is related to the small interface of β‐barrel domains. In addition, MreC forms an antiparallel filament‐like structure along the coiled‐coil direction, which is different from the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC.
abstract_unstemmed	MreC is a scaffold protein required for cell shape determination through interactions with proteins related to cell wall synthesis. Here, we determined the crystal structure of the major periplasmic part of MreC from Escherichia coli at 2.1 Å resolution. The periplasmic part of MreC contains a coiled‐coil domain and two six‐stranded barrel domains. The coiled‐coil domain is essential for dimer formation, and the two monomers are prone to relative motion that is related to the small interface of β‐barrel domains. In addition, MreC forms an antiparallel filament‐like structure along the coiled‐coil direction, which is different from the helical array structure in Pseudomonas aeruginosa. Our structure deepens our understanding of polymer formation of MreC.
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title_short	The crystal structure of MreC provides insights into polymer formation
url	https://doi.org/10.1002/2211-5463.13296 https://doaj.org/article/689707c1a13b4ccd84a6e8fcfaa1a6cf https://doaj.org/toc/2211-5463
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The crystal structure of MreC provides insights into polymer formation

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