A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin
Abstract The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl‐chain recognition in any membrane‐bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps path...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Ahn, Victoria E [verfasserIn] Lo, Eileen I [verfasserIn] Engel, Christian K [verfasserIn] Chen, Lu [verfasserIn] Hwang, Peter M [verfasserIn] Kay, Lewis E [verfasserIn] Bishop, Russell E [verfasserIn] Privé, Gilbert G [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2004 |
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| Schlagwörter: |
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| Anmerkung: |
© European Molecular Biology Organization 2004 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 23(2004), 15 vom: 22. Juli, Seite 2931-2941 |
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| Übergeordnetes Werk: |
volume:23 ; year:2004 ; number:15 ; day:22 ; month:07 ; pages:2931-2941 |
| Links: |
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| DOI / URN: |
10.1038/sj.emboj.7600320 |
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| Katalog-ID: |
SPR058134743 |
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| 024 | 7 | |a 10.1038/sj.emboj.7600320 |2 doi | |
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| 041 | |a eng | ||
| 100 | 1 | |a Ahn, Victoria E |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin |
| 264 | 1 | |c 2004 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
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| 500 | |a © European Molecular Biology Organization 2004 | ||
| 520 | |a Abstract The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl‐chain recognition in any membrane‐bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 Å crystal structure of PagP, an eight‐stranded β‐barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP β‐barrel axis is tilted by approximately 25°. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. A striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins. | ||
| 650 | 4 | |a crystal structure |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a endotoxin |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a lipid A |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a phospholipids |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a signal transduction |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Lo, Eileen I |e verfasserin |4 aut | |
| 700 | 1 | |a Engel, Christian K |e verfasserin |4 aut | |
| 700 | 1 | |a Chen, Lu |e verfasserin |4 aut | |
| 700 | 1 | |a Hwang, Peter M |e verfasserin |4 aut | |
| 700 | 1 | |a Kay, Lewis E |e verfasserin |4 aut | |
| 700 | 1 | |a Bishop, Russell E |e verfasserin |4 aut | |
| 700 | 1 | |a Privé, Gilbert G |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t The EMBO Journal |d Nature Publishing Group UK, 2023 |g 23(2004), 15 vom: 22. Juli, Seite 2931-2941 |w (DE-627)266022529 |w (DE-600)1467419-1 |x 1460-2075 |7 nnns |
| 773 | 1 | 8 | |g volume:23 |g year:2004 |g number:15 |g day:22 |g month:07 |g pages:2931-2941 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.1038/sj.emboj.7600320 |m X:SPRINGER |x Resolving-System |z lizenzpflichtig |3 Volltext |
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| 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 | ||
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| 912 | |a GBV_ILN_4305 | ||
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| 912 | |a GBV_ILN_4314 | ||
| 912 | |a GBV_ILN_4315 | ||
| 912 | |a GBV_ILN_4317 | ||
| 912 | |a GBV_ILN_4318 | ||
| 912 | |a GBV_ILN_4322 | ||
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| 912 | |a GBV_ILN_4324 | ||
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| 951 | |a AR | ||
| 952 | |d 23 |j 2004 |e 15 |b 22 |c 07 |h 2931-2941 | ||
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2004 |
| publishDate |
2004 |
| allfields |
10.1038/sj.emboj.7600320 doi (DE-627)SPR058134743 (SPR)sj.emboj.7600320-e DE-627 ger DE-627 rakwb eng Ahn, Victoria E verfasserin aut A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin 2004 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2004 Abstract The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl‐chain recognition in any membrane‐bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 Å crystal structure of PagP, an eight‐stranded β‐barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP β‐barrel axis is tilted by approximately 25°. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. A striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins. crystal structure (dpeaa)DE-He213 endotoxin (dpeaa)DE-He213 lipid A (dpeaa)DE-He213 phospholipids (dpeaa)DE-He213 signal transduction (dpeaa)DE-He213 Lo, Eileen I verfasserin aut Engel, Christian K verfasserin aut Chen, Lu verfasserin aut Hwang, Peter M verfasserin aut Kay, Lewis E verfasserin aut Bishop, Russell E verfasserin aut Privé, Gilbert G verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 23(2004), 15 vom: 22. Juli, Seite 2931-2941 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:23 year:2004 number:15 day:22 month:07 pages:2931-2941 https://dx.doi.org/10.1038/sj.emboj.7600320 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER 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_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_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 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_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 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_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4318 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_4598 GBV_ILN_4700 AR 23 2004 15 22 07 2931-2941 |
| spelling |
10.1038/sj.emboj.7600320 doi (DE-627)SPR058134743 (SPR)sj.emboj.7600320-e DE-627 ger DE-627 rakwb eng Ahn, Victoria E verfasserin aut A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin 2004 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2004 Abstract The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl‐chain recognition in any membrane‐bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 Å crystal structure of PagP, an eight‐stranded β‐barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP β‐barrel axis is tilted by approximately 25°. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. A striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins. crystal structure (dpeaa)DE-He213 endotoxin (dpeaa)DE-He213 lipid A (dpeaa)DE-He213 phospholipids (dpeaa)DE-He213 signal transduction (dpeaa)DE-He213 Lo, Eileen I verfasserin aut Engel, Christian K verfasserin aut Chen, Lu verfasserin aut Hwang, Peter M verfasserin aut Kay, Lewis E verfasserin aut Bishop, Russell E verfasserin aut Privé, Gilbert G verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 23(2004), 15 vom: 22. Juli, Seite 2931-2941 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:23 year:2004 number:15 day:22 month:07 pages:2931-2941 https://dx.doi.org/10.1038/sj.emboj.7600320 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER 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_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_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 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_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 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_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4318 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_4598 GBV_ILN_4700 AR 23 2004 15 22 07 2931-2941 |
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10.1038/sj.emboj.7600320 doi (DE-627)SPR058134743 (SPR)sj.emboj.7600320-e DE-627 ger DE-627 rakwb eng Ahn, Victoria E verfasserin aut A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin 2004 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2004 Abstract The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl‐chain recognition in any membrane‐bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 Å crystal structure of PagP, an eight‐stranded β‐barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP β‐barrel axis is tilted by approximately 25°. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. A striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins. crystal structure (dpeaa)DE-He213 endotoxin (dpeaa)DE-He213 lipid A (dpeaa)DE-He213 phospholipids (dpeaa)DE-He213 signal transduction (dpeaa)DE-He213 Lo, Eileen I verfasserin aut Engel, Christian K verfasserin aut Chen, Lu verfasserin aut Hwang, Peter M verfasserin aut Kay, Lewis E verfasserin aut Bishop, Russell E verfasserin aut Privé, Gilbert G verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 23(2004), 15 vom: 22. Juli, Seite 2931-2941 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:23 year:2004 number:15 day:22 month:07 pages:2931-2941 https://dx.doi.org/10.1038/sj.emboj.7600320 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER 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_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_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 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_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 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_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4318 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_4598 GBV_ILN_4700 AR 23 2004 15 22 07 2931-2941 |
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10.1038/sj.emboj.7600320 doi (DE-627)SPR058134743 (SPR)sj.emboj.7600320-e DE-627 ger DE-627 rakwb eng Ahn, Victoria E verfasserin aut A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin 2004 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2004 Abstract The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl‐chain recognition in any membrane‐bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 Å crystal structure of PagP, an eight‐stranded β‐barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP β‐barrel axis is tilted by approximately 25°. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. A striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins. crystal structure (dpeaa)DE-He213 endotoxin (dpeaa)DE-He213 lipid A (dpeaa)DE-He213 phospholipids (dpeaa)DE-He213 signal transduction (dpeaa)DE-He213 Lo, Eileen I verfasserin aut Engel, Christian K verfasserin aut Chen, Lu verfasserin aut Hwang, Peter M verfasserin aut Kay, Lewis E verfasserin aut Bishop, Russell E verfasserin aut Privé, Gilbert G verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 23(2004), 15 vom: 22. Juli, Seite 2931-2941 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:23 year:2004 number:15 day:22 month:07 pages:2931-2941 https://dx.doi.org/10.1038/sj.emboj.7600320 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER 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_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_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 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_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 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_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4318 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_4598 GBV_ILN_4700 AR 23 2004 15 22 07 2931-2941 |
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10.1038/sj.emboj.7600320 doi (DE-627)SPR058134743 (SPR)sj.emboj.7600320-e DE-627 ger DE-627 rakwb eng Ahn, Victoria E verfasserin aut A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin 2004 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2004 Abstract The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl‐chain recognition in any membrane‐bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 Å crystal structure of PagP, an eight‐stranded β‐barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP β‐barrel axis is tilted by approximately 25°. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. A striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins. crystal structure (dpeaa)DE-He213 endotoxin (dpeaa)DE-He213 lipid A (dpeaa)DE-He213 phospholipids (dpeaa)DE-He213 signal transduction (dpeaa)DE-He213 Lo, Eileen I verfasserin aut Engel, Christian K verfasserin aut Chen, Lu verfasserin aut Hwang, Peter M verfasserin aut Kay, Lewis E verfasserin aut Bishop, Russell E verfasserin aut Privé, Gilbert G verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 23(2004), 15 vom: 22. Juli, Seite 2931-2941 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:23 year:2004 number:15 day:22 month:07 pages:2931-2941 https://dx.doi.org/10.1038/sj.emboj.7600320 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER 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_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_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 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_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 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_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4318 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_4598 GBV_ILN_4700 AR 23 2004 15 22 07 2931-2941 |
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Enthalten in The EMBO Journal 23(2004), 15 vom: 22. Juli, Seite 2931-2941 volume:23 year:2004 number:15 day:22 month:07 pages:2931-2941 |
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Ahn, Victoria E @@aut@@ Lo, Eileen I @@aut@@ Engel, Christian K @@aut@@ Chen, Lu @@aut@@ Hwang, Peter M @@aut@@ Kay, Lewis E @@aut@@ Bishop, Russell E @@aut@@ Privé, Gilbert G @@aut@@ |
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PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 Å crystal structure of PagP, an eight‐stranded β‐barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP β‐barrel axis is tilted by approximately 25°. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. 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Ahn, Victoria E |
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Ahn, Victoria E misc crystal structure misc endotoxin misc lipid A misc phospholipids misc signal transduction A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin |
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A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin crystal structure (dpeaa)DE-He213 endotoxin (dpeaa)DE-He213 lipid A (dpeaa)DE-He213 phospholipids (dpeaa)DE-He213 signal transduction (dpeaa)DE-He213 |
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A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin |
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Ahn, Victoria E Lo, Eileen I Engel, Christian K Chen, Lu Hwang, Peter M Kay, Lewis E Bishop, Russell E Privé, Gilbert G |
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a hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin |
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A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin |
| abstract |
Abstract The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl‐chain recognition in any membrane‐bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 Å crystal structure of PagP, an eight‐stranded β‐barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP β‐barrel axis is tilted by approximately 25°. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. A striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins. © European Molecular Biology Organization 2004 |
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Abstract The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl‐chain recognition in any membrane‐bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 Å crystal structure of PagP, an eight‐stranded β‐barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP β‐barrel axis is tilted by approximately 25°. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. A striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins. © European Molecular Biology Organization 2004 |
| abstract_unstemmed |
Abstract The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl‐chain recognition in any membrane‐bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 Å crystal structure of PagP, an eight‐stranded β‐barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP β‐barrel axis is tilted by approximately 25°. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. A striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins. © European Molecular Biology Organization 2004 |
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A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin |
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https://dx.doi.org/10.1038/sj.emboj.7600320 |
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Lo, Eileen I Engel, Christian K Chen, Lu Hwang, Peter M Kay, Lewis E Bishop, Russell E Privé, Gilbert G |
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10.1038/sj.emboj.7600320 |
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2024-10-28T07:09:01.221Z |
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| score |
7.4011803 |