Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels

The P-type ATPase subunit KdpB of KdpFABC hydrolyzes ATP while K+ transport was assumed to occur through channel-like subunit KdpA. Here, the authors show two cryo-EM structures of KdpFABC which suggest a translocation pathway through two inter-subunit half-channels formed by KdpA and KdpB.

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Autores principales:	C. Stock, L. Hielkema, I. Tascón, D. Wunnicke, G. T. Oostergetel, M. Azkargorta, C. Paulino, I. Hänelt
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/56ab652f6ae74938964ac89a3f6d6f3e
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spelling	oai:doaj.org-article:56ab652f6ae74938964ac89a3f6d6f3e2021-12-02T17:31:28ZCryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels10.1038/s41467-018-07319-22041-1723https://doaj.org/article/56ab652f6ae74938964ac89a3f6d6f3e2018-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07319-2https://doaj.org/toc/2041-1723The P-type ATPase subunit KdpB of KdpFABC hydrolyzes ATP while K+ transport was assumed to occur through channel-like subunit KdpA. Here, the authors show two cryo-EM structures of KdpFABC which suggest a translocation pathway through two inter-subunit half-channels formed by KdpA and KdpB.C. StockL. HielkemaI. TascónD. WunnickeG. T. OostergetelM. AzkargortaC. PaulinoI. HäneltNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q C. Stock L. Hielkema I. Tascón D. Wunnicke G. T. Oostergetel M. Azkargorta C. Paulino I. Hänelt Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels
description	The P-type ATPase subunit KdpB of KdpFABC hydrolyzes ATP while K+ transport was assumed to occur through channel-like subunit KdpA. Here, the authors show two cryo-EM structures of KdpFABC which suggest a translocation pathway through two inter-subunit half-channels formed by KdpA and KdpB.
format	article
author	C. Stock L. Hielkema I. Tascón D. Wunnicke G. T. Oostergetel M. Azkargorta C. Paulino I. Hänelt
author_facet	C. Stock L. Hielkema I. Tascón D. Wunnicke G. T. Oostergetel M. Azkargorta C. Paulino I. Hänelt
author_sort	C. Stock
title	Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels
title_short	Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels
title_full	Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels
title_fullStr	Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels
title_full_unstemmed	Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels
title_sort	cryo-em structures of kdpfabc suggest a k+ transport mechanism via two inter-subunit half-channels
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/56ab652f6ae74938964ac89a3f6d6f3e
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Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels

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