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- W2045017092 abstract "Uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes a reversible reaction for adding an O-acyl group to the GlcNAc in UDP-GlcNAc in the first step of lipid A biosynthesis. Lipid A constitutes a major component of lipopolysaccharides, also referred to as endotoxins, which form the outer monolayer of the outer membrane of Gram-negative bacteria. Ligand-free and UDP-GlcNAc-bound crystal structures of LpxA from Bacteroides fragilis NCTC 9343, the most common pathogenic bacteria found in abdominal abscesses, have been determined and are presented here. The enzyme crystallizes in a cubic space group, with the crystallographic threefold axis generating the biological functional homotrimer and with each monomer forming a nine-rung left-handed β-helical (LβH) fold in the N-terminus followed by an α-helical motif in the C-terminus. The structure is highly similar to LpxA from other organisms. Yet, despite sharing a similar LβH structure with LpxAs from Escherichia coli and others, previously unseen calcium ions are observed on the threefold axis in B. fragilis LpxA to help stabilize the trimeric assembly." @default.
- W2045017092 created "2016-06-24" @default.
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- W2045017092 date "2015-04-24" @default.
- W2045017092 modified "2023-10-18" @default.
- W2045017092 title "Structures of<i>Bacteroides fragilis</i>uridine 5′-diphosphate-<i>N</i>-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA)" @default.
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- W2045017092 doi "https://doi.org/10.1107/s1399004715003326" @default.
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