Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis.
Abstract
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.
Type
Journal articlePermalink
https://hdl.handle.net/10161/13058Published Version (Please cite this version)
10.1038/nmicrobiol.2016.154Publication Info
Cho, Jae; Lee, Chul-Jin; Zhao, Jinshi; Young, Hayley E; & Zhou, Pei (2016). Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase
LpxH in lipid A biosynthesis. Nat Microbiol, 1(11). pp. 16154. 10.1038/nmicrobiol.2016.154. Retrieved from https://hdl.handle.net/10161/13058.This is constructed from limited available data and may be imprecise. To cite this
article, please review & use the official citation provided by the journal.
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Show full item recordScholars@Duke
Pei Zhou
Professor of Biochemistry
Protein-protein interactions play a pivotal role in the regulation of various cellular
processes. The formation of higher order protein complexes is frequently accompanied
by extensive structural remodeling of the individual components, varying from domain
re-orientation to induced folding of unstructured elements. Nuclear Magnetic Resonance
(NMR) spectroscopy is a powerful tool for macromolecular structure determination in
solution. It has the unique advantage of being capable of elucidati

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