Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus

H+-ATPases employ a rotary catalytic mechanism to couple ATP synthesis/hydrolysis with proton translocation through the membrane. Here, the authors use high-resolution cryoEM to characterize three rotational states of a bacterial H+-ATPase, providing a more detailed model of its catalytic mechanism.

Guardado en:

Detalles Bibliográficos
Autores principales:	Atsuko Nakanishi, Jun-ichi Kishikawa, Masatada Tamakoshi, Kaoru Mitsuoka, Ken Yokoyama
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/cfecab94ebe5407db9477c180e68a42b
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:cfecab94ebe5407db9477c180e68a42b
record_format	dspace
spelling	oai:doaj.org-article:cfecab94ebe5407db9477c180e68a42b2021-12-02T15:33:47ZCryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus10.1038/s41467-017-02553-62041-1723https://doaj.org/article/cfecab94ebe5407db9477c180e68a42b2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02553-6https://doaj.org/toc/2041-1723H+-ATPases employ a rotary catalytic mechanism to couple ATP synthesis/hydrolysis with proton translocation through the membrane. Here, the authors use high-resolution cryoEM to characterize three rotational states of a bacterial H+-ATPase, providing a more detailed model of its catalytic mechanism.Atsuko NakanishiJun-ichi KishikawaMasatada TamakoshiKaoru MitsuokaKen YokoyamaNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Atsuko Nakanishi Jun-ichi Kishikawa Masatada Tamakoshi Kaoru Mitsuoka Ken Yokoyama Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus
description	H+-ATPases employ a rotary catalytic mechanism to couple ATP synthesis/hydrolysis with proton translocation through the membrane. Here, the authors use high-resolution cryoEM to characterize three rotational states of a bacterial H+-ATPase, providing a more detailed model of its catalytic mechanism.
format	article
author	Atsuko Nakanishi Jun-ichi Kishikawa Masatada Tamakoshi Kaoru Mitsuoka Ken Yokoyama
author_facet	Atsuko Nakanishi Jun-ichi Kishikawa Masatada Tamakoshi Kaoru Mitsuoka Ken Yokoyama
author_sort	Atsuko Nakanishi
title	Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus
title_short	Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus
title_full	Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus
title_fullStr	Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus
title_full_unstemmed	Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus
title_sort	cryo em structure of intact rotary h+-atpase/synthase from thermus thermophilus
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/cfecab94ebe5407db9477c180e68a42b
work_keys_str_mv	AT atsukonakanishi cryoemstructureofintactrotaryhatpasesynthasefromthermusthermophilus AT junichikishikawa cryoemstructureofintactrotaryhatpasesynthasefromthermusthermophilus AT masatadatamakoshi cryoemstructureofintactrotaryhatpasesynthasefromthermusthermophilus AT kaorumitsuoka cryoemstructureofintactrotaryhatpasesynthasefromthermusthermophilus AT kenyokoyama cryoemstructureofintactrotaryhatpasesynthasefromthermusthermophilus
_version_	1718387050841899008

Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus

Ejemplares similares