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.

Guardado en:
Detalles Bibliográficos
Autores principales: Sean D. Workman, Liam J. Worrall, Natalie C. J. Strynadka
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
Materias:
Q
Acceso en línea:https://doaj.org/article/2e86e17751974345a1a2d3a330963722
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:2e86e17751974345a1a2d3a330963722
record_format dspace
spelling oai:doaj.org-article:2e86e17751974345a1a2d3a3309637222021-12-02T16:49:34ZCrystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling10.1038/s41467-018-03547-82041-1723https://doaj.org/article/2e86e17751974345a1a2d3a3309637222018-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03547-8https://doaj.org/toc/2041-1723Undecaprenyl 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.Sean D. WorkmanLiam J. WorrallNatalie C. J. StrynadkaNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
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.
format article
author Sean D. Workman
Liam J. Worrall
Natalie C. J. Strynadka
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 Portfolio
publishDate 2018
url https://doaj.org/article/2e86e17751974345a1a2d3a330963722
work_keys_str_mv AT seandworkman crystalstructureofanintramembranalphosphatasecentraltobacterialcellwallpeptidoglycanbiosynthesisandlipidrecycling
AT liamjworrall crystalstructureofanintramembranalphosphatasecentraltobacterialcellwallpeptidoglycanbiosynthesisandlipidrecycling
AT nataliecjstrynadka crystalstructureofanintramembranalphosphatasecentraltobacterialcellwallpeptidoglycanbiosynthesisandlipidrecycling
_version_ 1718383268355637248