Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis.
Published online
Journal Article
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 inhibition of LpxH.
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Duke Authors
Cited Authors
- Cho, J; Lee, C-J; Zhao, J; Young, HE; Zhou, P
Published Date
- August 15, 2016
Published In
Volume / Issue
- 1 / 11
Start / End Page
- 16154 -
PubMed ID
- 27780190
Pubmed Central ID
- 27780190
Electronic International Standard Serial Number (EISSN)
- 2058-5276
Digital Object Identifier (DOI)
- 10.1038/nmicrobiol.2016.154
Language
- eng
Conference Location
- England