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Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis.

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Cho_LpxH_Nature_Microbiol_2016.pdf
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Date
2016-08-15
Authors
Cho, Jae
Lee, Chul-Jin
Zhao, Jinshi
Young, Hayley E
Zhou, Pei
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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 article
Permalink
https://hdl.handle.net/10161/13058
Published Version (Please cite this version)
10.1038/nmicrobiol.2016.154
Publication 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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Scholars@Duke

Zhou

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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