Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch

F1Fo ATP synthase consists of two coupled rotary molecular motors: the soluble ATPase F1 and the transmembrane Fo. Here, the authors present cryo-EM structures of E. coli ATP synthase in four discrete rotational sub-states at 3.1-3.4 Å resolution and observe a rotary sub-step of the Fo motor cring t...

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Autores principales:	Meghna Sobti, James L. Walshe, Di Wu, Robert Ishmukhametov, Yi C. Zeng, Carol V. Robinson, Richard M. Berry, Alastair G. Stewart
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0173de1fc389481f868feeaeaacc4180
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id	oai:doaj.org-article:0173de1fc389481f868feeaeaacc4180
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spelling	oai:doaj.org-article:0173de1fc389481f868feeaeaacc41802021-12-02T16:53:07ZCryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch10.1038/s41467-020-16387-22041-1723https://doaj.org/article/0173de1fc389481f868feeaeaacc41802020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16387-2https://doaj.org/toc/2041-1723F1Fo ATP synthase consists of two coupled rotary molecular motors: the soluble ATPase F1 and the transmembrane Fo. Here, the authors present cryo-EM structures of E. coli ATP synthase in four discrete rotational sub-states at 3.1-3.4 Å resolution and observe a rotary sub-step of the Fo motor cring that reveals the mechanism of elastic coupling between the two rotary motors, which is essential for effective ATP synthesis.Meghna SobtiJames L. WalsheDi WuRobert IshmukhametovYi C. ZengCarol V. RobinsonRichard M. BerryAlastair G. StewartNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Meghna Sobti James L. Walshe Di Wu Robert Ishmukhametov Yi C. Zeng Carol V. Robinson Richard M. Berry Alastair G. Stewart Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch
description	F1Fo ATP synthase consists of two coupled rotary molecular motors: the soluble ATPase F1 and the transmembrane Fo. Here, the authors present cryo-EM structures of E. coli ATP synthase in four discrete rotational sub-states at 3.1-3.4 Å resolution and observe a rotary sub-step of the Fo motor cring that reveals the mechanism of elastic coupling between the two rotary motors, which is essential for effective ATP synthesis.
format	article
author	Meghna Sobti James L. Walshe Di Wu Robert Ishmukhametov Yi C. Zeng Carol V. Robinson Richard M. Berry Alastair G. Stewart
author_facet	Meghna Sobti James L. Walshe Di Wu Robert Ishmukhametov Yi C. Zeng Carol V. Robinson Richard M. Berry Alastair G. Stewart
author_sort	Meghna Sobti
title	Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch
title_short	Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch
title_full	Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch
title_fullStr	Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch
title_full_unstemmed	Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch
title_sort	cryo-em structures provide insight into how e. coli f1fo atp synthase accommodates symmetry mismatch
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/0173de1fc389481f868feeaeaacc4180
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Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch

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