Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 104, Issue 34, Pages 13543-13550Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0705833104
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- NIGMS NIH HHS [GM-51310, R01 GM051310] Funding Source: Medline
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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 P-helix fold. We have now solved the crystal structures of E. coli LpxA with the bound product UDP-3-O-(R-3-hydroxymyristoyl)-GicNAc at a resolution of 1.74 angstrom and with bound UDP-3-O-(R-3-hydroxydecanoyl)GlcNAc at 1.85 angstrom. The structures of these complexes are consistent with the catalytic mechanism deduced by mutagenesis and with a recent 3.0-angstrom 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.
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