6s3k

Publication Abstract from PubMed

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 A 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.

Structural basis of proton-coupled potassium transport in the KUP family.,Tascon I, Sousa JS, Corey RA, Mills DJ, Griwatz D, Aumuller N, Mikusevic V, Stansfeld PJ, Vonck J, Hanelt I Nat Commun. 2020 Jan 31;11(1):626. doi: 10.1038/s41467-020-14441-7. PMID:32005818^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.