{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":58,"searchCount":0},"additional":{"submitter":["Tascon I"],"funding":["RCUK | Engineering and Physical Sciences Research Council (EPSRC)","Deutsche Forschungsgemeinschaft","Medical Research Council","RCUK | Biotechnology and Biological Sciences Research Council","RCUK | Medical Research Council","RCUK | Engineering and Physical Sciences Research Council","Cluster of Excellence Macromolecular Complexes, Frankfurt","Biotechnology and Biological Sciences Research Council","Max-Planck-Gesellschaft","Engineering and Physical Sciences Research Council"],"pagination":["626"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6994465"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(1)"],"pubmed_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<sup>+</sup>/H<sup>+</sup> 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."],"journal":["Nature communications"],"pubmed_title":["Structural basis of proton-coupled potassium transport in the KUP family."],"pmcid":["PMC6994465"],"funding_grant_id":["HA 6322/4-1, VO 1449/1-1","BB/S003339/1","BB/P01948X/1, BB/R002517/1 BB/S003339/1","BB/P01948X/2","BB/P01948X/1","EP/R029407/1","MR/S009213/1","BB/R002517/1"],"pubmed_authors":["Corey RA","Mills DJ","Aumuller N","Tascon I","Vonck J","Hanelt I","Mikusevic V","Sousa JS","Griwatz D","Stansfeld PJ"],"view_count":["58"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis of proton-coupled potassium transport in the KUP family.","description":"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<sup>+</sup>/H<sup>+</sup> 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.","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jan","modification":"2024-11-13T12:56:34.063Z","creation":"2020-05-22T09:31:33Z"},"accession":"S-EPMC6994465","cross_references":{"pubmed":["32005818"],"doi":["10.1038/s41467-020-14441-7"]}}