1thq
From Proteopedia
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|PDB= 1thq |SIZE=350|CAPTION= <scene name='initialview01'>1thq</scene>, resolution 1.90Å | |PDB= 1thq |SIZE=350|CAPTION= <scene name='initialview01'>1thq</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CRCA, B0622 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= CRCA, B0622 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1mm4|1MM4]], [[1mm5|1MM5]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1thq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1thq OCA], [http://www.ebi.ac.uk/pdbsum/1thq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1thq RCSB]</span> | ||
}} | }} | ||
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[[Category: Lo, E I.]] | [[Category: Lo, E I.]] | ||
[[Category: Prive, G G.]] | [[Category: Prive, G G.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: LDA]] | ||
| - | [[Category: MPD]] | ||
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
[[Category: outer membrane enzyme]] | [[Category: outer membrane enzyme]] | ||
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[[Category: palmitoyltransferase]] | [[Category: palmitoyltransferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:56:13 2008'' |
Revision as of 20:56, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | CRCA, B0622 (Escherichia coli) | ||||||
| Related: | 1MM4, 1MM5
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Outer Membrane Enzyme PagP
Overview
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 A crystal structure of PagP, an eight-stranded beta-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 beta-barrel axis is tilted by approximately 25 degrees. 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.
About this Structure
1THQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin., Ahn VE, Lo EI, Engel CK, Chen L, Hwang PM, Kay LE, Bishop RE, Prive GG, EMBO J. 2004 Aug 4;23(15):2931-41. Epub 2004 Jul 22. PMID:15272304
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