Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis

Bacterial cell wall components are assembled in a transmembrane cycle that involves the membrane integral pyrophosphorylase, BacA. Here the authors solve the crystal structure of BacA which shows an interdigitated inverted topology repeat that hints towards a flippase function for BacA.

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Autores principales:	Meriem El Ghachi, Nicole Howe, Chia-Ying Huang, Vincent Olieric, Rangana Warshamanage, Thierry Touzé, Dietmar Weichert, Phillip J. Stansfeld, Meitian Wang, Fred Kerff, Martin Caffrey
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/987e6a420d7e43b5beb6875d278ef2d9
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spelling	oai:doaj.org-article:987e6a420d7e43b5beb6875d278ef2d92021-12-02T17:33:05ZCrystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis10.1038/s41467-018-03477-52041-1723https://doaj.org/article/987e6a420d7e43b5beb6875d278ef2d92018-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03477-5https://doaj.org/toc/2041-1723Bacterial cell wall components are assembled in a transmembrane cycle that involves the membrane integral pyrophosphorylase, BacA. Here the authors solve the crystal structure of BacA which shows an interdigitated inverted topology repeat that hints towards a flippase function for BacA.Meriem El GhachiNicole HoweChia-Ying HuangVincent OliericRangana WarshamanageThierry TouzéDietmar WeichertPhillip J. StansfeldMeitian WangFred KerffMartin CaffreyNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Meriem El Ghachi Nicole Howe Chia-Ying Huang Vincent Olieric Rangana Warshamanage Thierry Touzé Dietmar Weichert Phillip J. Stansfeld Meitian Wang Fred Kerff Martin Caffrey Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
description	Bacterial cell wall components are assembled in a transmembrane cycle that involves the membrane integral pyrophosphorylase, BacA. Here the authors solve the crystal structure of BacA which shows an interdigitated inverted topology repeat that hints towards a flippase function for BacA.
format	article
author	Meriem El Ghachi Nicole Howe Chia-Ying Huang Vincent Olieric Rangana Warshamanage Thierry Touzé Dietmar Weichert Phillip J. Stansfeld Meitian Wang Fred Kerff Martin Caffrey
author_facet	Meriem El Ghachi Nicole Howe Chia-Ying Huang Vincent Olieric Rangana Warshamanage Thierry Touzé Dietmar Weichert Phillip J. Stansfeld Meitian Wang Fred Kerff Martin Caffrey
author_sort	Meriem El Ghachi
title	Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
title_short	Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
title_full	Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
title_fullStr	Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
title_full_unstemmed	Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
title_sort	crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/987e6a420d7e43b5beb6875d278ef2d9
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Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis

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