2qiv
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(New page: 200px<br /><applet load="2qiv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qiv, resolution 1.850Å" /> '''Structural basis fo...)
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Revision as of 11:21, 23 January 2008
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Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase
Overview
UDP-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes the, first step of lipid A biosynthesis, the reversible transfer of the, R-3-hydroxyacyl chain from R-3-hydroxyacyl acyl carrier protein to the, glucosamine 3-OH group of UDP-GlcNAc. Escherichia coli LpxA is highly, selective for R-3-hydroxymyristate. The crystal structure of the E. coli, LpxA homotrimer, determined previously in the absence of lipid substrates, or products, revealed that LpxA contains an unusual, left-handed parallel, beta-helix fold. We have now solved the crystal structures of E. coli LpxA, with the bound product UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc at a, resolution of 1.74 A and with bound UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc, at 1.85 A. The structures of these complexes are consistent with the, catalytic mechanism deduced by mutagenesis and with a recent 3.0-A, structure of LpxA with bound UDP-GlcNAc. Our structures show how LpxA, selects for 14-carbon R-3-hydroxyacyl chains and reveal two modes of UDP, binding.
About this Structure
2QIV is a Single protein structure of sequence from Escherichia coli with as ligand. Active as [acyl-carrier-protein--UDP-N-acetylglucosamine_O-acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase], with EC number 2.3.1.129 Full crystallographic information is available from OCA.
Reference
Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase., Williams AH, Raetz CR, Proc Natl Acad Sci U S A. 2007 Aug 21;104(34):13543-50. Epub 2007 Aug 13. PMID:17698807 [[Category: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase]]
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