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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Auteurs principaux: Igor Tascón, Joana S. Sousa, Robin A. Corey, Deryck J. Mills, David Griwatz, Nadine Aumüller, Vedrana Mikusevic, Phillip J. Stansfeld, Janet Vonck, Inga Hänelt
Format: article
Langue:EN
Publié: Nature Portfolio 2020
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Accès en ligne:https://doaj.org/article/5078592bb5b64359bd80dda185a44d08
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Résumé: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.