Structural basis of proton-coupled potassium transport in the KUP family

KUP transporters facilitate potassium uptake by the co-transport of protons and are key players in potassium homeostasis. Here authors identify the potassium importer KimA from Bacillus subtilis as a new member of the KUP transporter family and show the cryo-EM structure of KimA in an inward-occlude...

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Autores principales:	Igor Tascón, Joana S. Sousa, Robin A. Corey, Deryck J. Mills, David Griwatz, Nadine Aumüller, Vedrana Mikusevic, Phillip J. Stansfeld, Janet Vonck, Inga Hänelt
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5078592bb5b64359bd80dda185a44d08
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spelling	oai:doaj.org-article:5078592bb5b64359bd80dda185a44d082021-12-02T17:32:12ZStructural basis of proton-coupled potassium transport in the KUP family10.1038/s41467-020-14441-72041-1723https://doaj.org/article/5078592bb5b64359bd80dda185a44d082020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14441-7https://doaj.org/toc/2041-1723KUP transporters facilitate potassium uptake by the co-transport of protons and are key players in potassium homeostasis. Here authors identify the potassium importer KimA from Bacillus subtilis as a new member of the KUP transporter family and show the cryo-EM structure of KimA in an inward-occluded, trans-inhibited conformation.Igor TascónJoana S. SousaRobin A. CoreyDeryck J. MillsDavid GriwatzNadine AumüllerVedrana MikusevicPhillip J. StansfeldJanet VonckInga HäneltNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Igor Tascón Joana S. Sousa Robin A. Corey Deryck J. Mills David Griwatz Nadine Aumüller Vedrana Mikusevic Phillip J. Stansfeld Janet Vonck Inga Hänelt Structural basis of proton-coupled potassium transport in the KUP family
description	KUP transporters facilitate potassium uptake by the co-transport of protons and are key players in potassium homeostasis. Here authors identify the potassium importer KimA from Bacillus subtilis as a new member of the KUP transporter family and show the cryo-EM structure of KimA in an inward-occluded, trans-inhibited conformation.
format	article
author	Igor Tascón Joana S. Sousa Robin A. Corey Deryck J. Mills David Griwatz Nadine Aumüller Vedrana Mikusevic Phillip J. Stansfeld Janet Vonck Inga Hänelt
author_facet	Igor Tascón Joana S. Sousa Robin A. Corey Deryck J. Mills David Griwatz Nadine Aumüller Vedrana Mikusevic Phillip J. Stansfeld Janet Vonck Inga Hänelt
author_sort	Igor Tascón
title	Structural basis of proton-coupled potassium transport in the KUP family
title_short	Structural basis of proton-coupled potassium transport in the KUP family
title_full	Structural basis of proton-coupled potassium transport in the KUP family
title_fullStr	Structural basis of proton-coupled potassium transport in the KUP family
title_full_unstemmed	Structural basis of proton-coupled potassium transport in the KUP family
title_sort	structural basis of proton-coupled potassium transport in the kup family
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/5078592bb5b64359bd80dda185a44d08
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Structural basis of proton-coupled potassium transport in the KUP family

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