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

Author

Listed:
  • 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
    University of Warwick)

  • Janet Vonck

    (Max Planck Institute of Biophysics)

  • Inga Hänelt

    (Goethe University Frankfurt)

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.

Suggested Citation

  • Igor Tascón & Joana S. Sousa & Robin A. Corey & Deryck J. Mills & David Griwatz & Nadine Aumüller & Vedrana Mikusevic & Phillip J. Stansfeld & Janet Vonck & Inga Hänelt, 2020. "Structural basis of proton-coupled potassium transport in the KUP family," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14441-7
    DOI: 10.1038/s41467-020-14441-7
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    Cited by:

    1. Tobias Maierhofer & Sönke Scherzer & Armando Carpaneto & Thomas D. Müller & Jose M. Pardo & Inga Hänelt & Dietmar Geiger & Rainer Hedrich, 2024. "Arabidopsis HAK5 under low K+ availability operates as PMF powered high-affinity K+ transporter," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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