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'''Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase''' | '''Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase''' | ||
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==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/17698807 17698807] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17698807 17698807] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Raetz, C R.H.]] | [[Category: Raetz, C R.H.]] | ||
[[Category: Williams, A H.]] | [[Category: Williams, A H.]] | ||
[[Category: | [[Category: Left-handed parallel beta helix]] | ||
[[Category: | [[Category: Protein lipid recognition]] | ||
[[Category: | [[Category: Transferase]] | ||
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Revision as of 12:02, 4 May 2008
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. 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 Page seeded by OCA on Sun May 4 15:02:02 2008
