Ontology highlight
ABSTRACT:
SUBMITTER: Cho J
PROVIDER: S-EPMC5081216 | biostudies-literature | 2016 Aug
REPOSITORIES: biostudies-literature
Cho Jae J Lee Chul-Jin CJ Zhao Jinshi J Young Hayley E HE Zhou Pei P
Nature microbiology 20160815 11
In most Gram-negative pathogens, the hydrolysis of UDP-2,3-diacylglucosamine to generate lipid X in lipid A biosynthesis is catalysed by the membrane-associated enzyme LpxH. We report the crystal structure of LpxH in complex with its product, lipid X, unveiling a unique insertion lid above the conserved architecture of calcineurin-like phosphoesterases. This structure reveals elaborate interactions surrounding lipid X and provides molecular insights into the substrate selectivity, catalysis and ...[more]