2b4q
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(New page: 200px<br /><applet load="2b4q" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b4q, resolution 2.30Å" /> '''Pseudomonas aerugino...)
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Revision as of 06:26, 21 November 2007
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Pseudomonas aeruginosa RhlG/NADP active-site complex
Overview
Rhamnolipids are extracellular biosurfactants and virulence factors, secreted by the opportunistic human pathogen Pseudomonas aeruginosa that, are required for swarming motility. The rhlG gene is essential for, rhamnolipid formation, and the RhlG enzyme is thought to divert fatty acid, synthesis intermediates into the rhamnolipid biosynthetic pathway based on, its similarity to FabG, the beta-ketoacyl-acyl carrier protein (ACP), reductase of type II fatty acid synthesis. Crystallographic analysis, reveals that the overall structures of the RhlG.NADP+ and FabG.NADP+, complexes are indeed similar, but there are key differences related to, function. RhlG does not undergo the conformational changes upon NADP(H), binding at the active site that in FabG are the structural basis of, negative allostery. Also, the acyl chain-binding pocket of RhlG is narrow, and rigid compared with the larger, flexible substrate-binding subdomain, in FabG. Finally, RhlG lacks a positively charged/hydrophobic surface, feature adjacent to the active site that is found on enzymes like FabG, that recognize the ACP of fatty acid synthesis. RhlG catalyzed the, NADPH-dependent reduction of beta-ketodecanoyl-ACP to, beta-d-hydroxydecanoyl-ACP. However, the enzyme was 2000-fold less active, than FabG in carrying out the same reaction. These structural and, biochemical studies establish RhlG as a NADPH-dependent beta-ketoacyl, reductase of the SDR protein superfamily and further suggest that the ACP, of fatty acid synthesis does not carry the substrates for RhlG.
About this Structure
2B4Q is a Single protein structure of sequence from Pseudomonas aeruginosa with NAP as ligand. Active as [acyl-carrier-protein_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number 1.1.1.100 Full crystallographic information is available from OCA.
Reference
Structure of RhlG, an essential beta-ketoacyl reductase in the rhamnolipid biosynthetic pathway of Pseudomonas aeruginosa., Miller DJ, Zhang YM, Rock CO, White SW, J Biol Chem. 2006 Jun 30;281(26):18025-32. Epub 2006 Apr 18. PMID:16624803 [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
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