Ontology highlight
ABSTRACT:
SUBMITTER: Williams AH
PROVIDER: S-EPMC1544142 | biostudies-literature | 2006 Jul
REPOSITORIES: biostudies-literature
Williams Allison H AH Immormino Robert M RM Gewirth Daniel T DT Raetz Christian R H CR
Proceedings of the National Academy of Sciences of the United States of America 20060711 29
UDP-GlcNAc acyltransferase (LpxA) catalyzes the first step of lipid A biosynthesis, the transfer of the R-3-hydroxyacyl chain from R-3-hydroxyacyl acyl carrier protein (ACP) to the glucosamine 3-OH group of UDP-GlcNAc. LpxA is essential for the growth of Escherichia coli and related Gram-negative bacteria. The crystal structure of the E. coli LpxA homotrimer, determined previously at 2.6 A in the absence of substrates or inhibitors, revealed that LpxA contains an unusual, left-handed parallel be ...[more]