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Tascón, Igor; Sousa, Joana S; Corey, Robin A; Mills, Deryck J; Griwatz, David; Aumüller, Nadine; Mikusevic, Vedrana; Stansfeld, Phillip J; Vonck, Janet; Hänelt, Inga
Nature communications, 01/2020, Letnik: 11, Številka: 1Journal Article
Potassium homeostasis is vital for all organisms, but is challenging in single-celled organisms like bacteria and yeast and immobile organisms like plants that constantly need to adapt to changing external conditions. KUP transporters facilitate potassium uptake by the co-transport of protons. Here, we uncover the molecular basis for transport in this widely distributed family. We identify the potassium importer KimA from Bacillus subtilis as a member of the KUP family, demonstrate that it functions as a K /H symporter and report a 3.7 Å cryo-EM structure of the KimA homodimer in an inward-occluded, trans-inhibited conformation. By introducing point mutations, we identify key residues for potassium and proton binding, which are conserved among other KUP proteins.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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