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

Tascón, I., Sousa, J. S., Corey, R. A., Mills, D. J., Griwatz, D., Aumüller, N., et al. (2020). Structural basis of proton-coupled potassium transport in the KUP family. Nature Communications, 11: 626. doi:10.1038/s41467-020-14441-7.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-9523-B Version Permalink: http://hdl.handle.net/21.11116/0000-0005-9524-A
Genre: Journal Article

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 Creators:
Tascón, Igor1, Author
Sousa, Joana S.2, Author              
Corey, Robin A.3, Author
Mills, Deryck J.2, Author              
Griwatz, David1, Author
Aumüller, Nadine1, Author
Mikusevic, Vedrana1, Author
Stansfeld, Phillip J.3, 4, Author
Vonck, Janet2, Author              
Hänelt, Inga1, Author
Affiliations:
1Institute of Biochemistry, Goethe University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
3Department of Biochemistry, University of Oxford, Oxford, UK, ou_persistent22              
4School of Life Sciences & Department of Chemistry, University of Warwick, Coventry, UK, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2019-08-222020-01-102020-01-31
 Publication Status: Published online
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41467-020-14441-7
BibTex Citekey: tascon_structural_2020
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 11 Sequence Number: 626 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723