Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling

Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling

Undecaprenyl pyrophosphate phosphatase (UppP) recycles the lipid carrier essential for bacterial cell wall synthesis. Here authors present the crystal structure of UppP from E. coli at 2.0 Å resolution, which sheds light on its phosphatase mechanism and indicates a potential flippase role for UppP.

Bibliographic Details
Main Authors: Sean D. Workman, Liam J. Worrall, Natalie C. J. Strynadka
Format: Article
Language:English
Published: Nature Publishing Group 2018-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-03547-8
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spelling doaj-2e86e17751974345a1a2d3a3309637222021-05-11T09:58:12ZengNature Publishing GroupNature Communications2041-17232018-03-01911910.1038/s41467-018-03547-8Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recyclingSean D. Workman0Liam J. Worrall1Natalie C. J. Strynadka2Department of Biochemistry and Molecular Biology and the Center for Blood Research, University of British ColumbiaDepartment of Biochemistry and Molecular Biology and the Center for Blood Research, University of British ColumbiaDepartment of Biochemistry and Molecular Biology and the Center for Blood Research, University of British ColumbiaUndecaprenyl pyrophosphate phosphatase (UppP) recycles the lipid carrier essential for bacterial cell wall synthesis. Here authors present the crystal structure of UppP from E. coli at 2.0 Å resolution, which sheds light on its phosphatase mechanism and indicates a potential flippase role for UppP.https://doi.org/10.1038/s41467-018-03547-8
collection DOAJ
language English
format Article
sources DOAJ
author Sean D. Workman
Liam J. Worrall
Natalie C. J. Strynadka
spellingShingle Sean D. Workman
Liam J. Worrall
Natalie C. J. Strynadka
Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling
Nature Communications
author_facet Sean D. Workman
Liam J. Worrall
Natalie C. J. Strynadka
author_sort Sean D. Workman
title Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling
title_short Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling
title_full Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling
title_fullStr Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling
title_full_unstemmed Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling
title_sort crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2018-03-01
description Undecaprenyl pyrophosphate phosphatase (UppP) recycles the lipid carrier essential for bacterial cell wall synthesis. Here authors present the crystal structure of UppP from E. coli at 2.0 Å resolution, which sheds light on its phosphatase mechanism and indicates a potential flippase role for UppP.
url https://doi.org/10.1038/s41467-018-03547-8
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AT liamjworrall crystalstructureofanintramembranalphosphatasecentraltobacterialcellwallpeptidoglycanbiosynthesisandlipidrecycling
AT nataliecjstrynadka crystalstructureofanintramembranalphosphatasecentraltobacterialcellwallpeptidoglycanbiosynthesisandlipidrecycling
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