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• W2052156598 endingPage "13550" @default.
• W2052156598 startingPage "13543" @default.
• W2052156598 abstract "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." @default.
• W2052156598 created "2016-06-24" @default.
• W2052156598 creator A5010161614 @default.
• W2052156598 creator A5087724371 @default.
• W2052156598 date "2007-08-21" @default.
• W2052156598 modified "2023-10-16" @default.
• W2052156598 title "Structural basis for the acyl chain selectivity and mechanism of UDP- <i>N</i> -acetylglucosamine acyltransferase" @default.
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• W2052156598 doi "https://doi.org/10.1073/pnas.0705833104" @default.
• W2052156598 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1959417" @default.
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