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

Loading...
Thumbnail Image

Date

2016-08-15

Journal Title

Journal ISSN

Volume Title

Repository Usage Stats

138
views
166
downloads

Citation Stats

Attention Stats

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.

Department

Description

Provenance

Subjects

Citation

Published Version (Please cite this version)

10.1038/nmicrobiol.2016.154

Publication Info

Cho, Jae, Chul-Jin Lee, Jinshi Zhao, Hayley E Young and Pei Zhou (2016). Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nat Microbiol, 1(11). p. 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.

Scholars@Duke

Zhou

Pei Zhou

Professor of Biochemistry

The Zhou lab focuses on the elucidation of the structure and dynamics of protein–protein and protein–ligand interactions and their functions in various cellular processes. Our current efforts are directed at enzymes and protein complexes involved in bacterial membrane biosynthesis, translesion DNA synthesis, co-transcriptional regulation, and host-pathogen interactions. Our investigations of these important cellular machineries have led to the development of novel antibiotics and cancer therapeutics, as well as the establishment of new biotechnology adventures.

 

The Zhou lab integrates a variety of biochemical and biophysical tools, including NMR, X-ray crystallography, cryo-EM, and enzymology. The lab has played a major role in the development and application of innovative NMR technologies, including high-resolution, high-dimensional spectral reconstruction techniques.


Unless otherwise indicated, scholarly articles published by Duke faculty members are made available here with a CC-BY-NC (Creative Commons Attribution Non-Commercial) license, as enabled by the Duke Open Access Policy. If you wish to use the materials in ways not already permitted under CC-BY-NC, please consult the copyright owner. Other materials are made available here through the author’s grant of a non-exclusive license to make their work openly accessible.