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

Igor Tascón, Joana S. Sousa, Robin A. Corey, Deryck J. Mills, David Griwatz, Nadine Aumüller, Vedrana Mikusevic, Phillip J. Stansfeld, Janet Vonck () and Inga Hänelt ()
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Igor Tascón: Goethe University Frankfurt
Joana S. Sousa: Max Planck Institute of Biophysics
Robin A. Corey: University of Oxford
Deryck J. Mills: Max Planck Institute of Biophysics
David Griwatz: Goethe University Frankfurt
Nadine Aumüller: Goethe University Frankfurt
Vedrana Mikusevic: Goethe University Frankfurt
Phillip J. Stansfeld: University of Oxford
Janet Vonck: Max Planck Institute of Biophysics
Inga Hänelt: Goethe University Frankfurt

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract 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.

Date: 2020
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DOI: 10.1038/s41467-020-14441-7

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