Structure and activation mechanism of the hexameric plasma membrane H+-ATPase

The plasma membrane H+ -ATPase is responsible for maintenance of the plasma membrane potential, which provides energy for the transport of nutrients, and the plasma membrane H+ -ATPase in S. cerevisiae (Pma1) is a P3A-type ATPase that assembles and functions as a hexamer. Here, the authors present t...

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Autores principales:	Peng Zhao, Chaoran Zhao, Dandan Chen, Caihong Yun, Huilin Li, Lin Bai
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ef9f9738c0284bd28fc377cd31762f9f
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spelling	oai:doaj.org-article:ef9f9738c0284bd28fc377cd31762f9f2021-11-14T12:36:53ZStructure and activation mechanism of the hexameric plasma membrane H+-ATPase10.1038/s41467-021-26782-y2041-1723https://doaj.org/article/ef9f9738c0284bd28fc377cd31762f9f2021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-26782-yhttps://doaj.org/toc/2041-1723The plasma membrane H+ -ATPase is responsible for maintenance of the plasma membrane potential, which provides energy for the transport of nutrients, and the plasma membrane H+ -ATPase in S. cerevisiae (Pma1) is a P3A-type ATPase that assembles and functions as a hexamer. Here, the authors present the cryo-EM structures of autoinhibited and activated native Pma1 hexamers purified with endogenous lipids and they propose a mechanism for proton pumping across the membrane by this family of H+ -ATPases.Peng ZhaoChaoran ZhaoDandan ChenCaihong YunHuilin LiLin BaiNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Peng Zhao Chaoran Zhao Dandan Chen Caihong Yun Huilin Li Lin Bai Structure and activation mechanism of the hexameric plasma membrane H+-ATPase
description	The plasma membrane H+ -ATPase is responsible for maintenance of the plasma membrane potential, which provides energy for the transport of nutrients, and the plasma membrane H+ -ATPase in S. cerevisiae (Pma1) is a P3A-type ATPase that assembles and functions as a hexamer. Here, the authors present the cryo-EM structures of autoinhibited and activated native Pma1 hexamers purified with endogenous lipids and they propose a mechanism for proton pumping across the membrane by this family of H+ -ATPases.
format	article
author	Peng Zhao Chaoran Zhao Dandan Chen Caihong Yun Huilin Li Lin Bai
author_facet	Peng Zhao Chaoran Zhao Dandan Chen Caihong Yun Huilin Li Lin Bai
author_sort	Peng Zhao
title	Structure and activation mechanism of the hexameric plasma membrane H+-ATPase
title_short	Structure and activation mechanism of the hexameric plasma membrane H+-ATPase
title_full	Structure and activation mechanism of the hexameric plasma membrane H+-ATPase
title_fullStr	Structure and activation mechanism of the hexameric plasma membrane H+-ATPase
title_full_unstemmed	Structure and activation mechanism of the hexameric plasma membrane H+-ATPase
title_sort	structure and activation mechanism of the hexameric plasma membrane h+-atpase
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/ef9f9738c0284bd28fc377cd31762f9f
work_keys_str_mv	AT pengzhao structureandactivationmechanismofthehexamericplasmamembranehatpase AT chaoranzhao structureandactivationmechanismofthehexamericplasmamembranehatpase AT dandanchen structureandactivationmechanismofthehexamericplasmamembranehatpase AT caihongyun structureandactivationmechanismofthehexamericplasmamembranehatpase AT huilinli structureandactivationmechanismofthehexamericplasmamembranehatpase AT linbai structureandactivationmechanismofthehexamericplasmamembranehatpase
_version_	1718429142741942272

Structure and activation mechanism of the hexameric plasma membrane H+-ATPase

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