6S3K

KimA from Bacillus subtilis in inward-facing, occluded state

Summary for 6S3K

• Entry DOI: 10.2210/pdb6s3k/pdb
• EMDB information: 10092
• Descriptor: APC family permease, POTASSIUM ION (2 entities in total)
• Functional Keywords: potassium transporter, leut fold, symporter, smalp, transport protein
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 133912.54

Authors

Tascon, I.,Sousa, J.S.,Vonck, J.,Haenelt, I. (deposition date: 2019-06-25, release date: 2020-02-12, Last modification date: 2024-05-22)

Primary citation

Tascon, I.,Sousa, J.S.,Corey, R.A.,Mills, D.J.,Griwatz, D.,Aumuller, N.,Mikusevic, V.,Stansfeld, P.J.,Vonck, J.,Hanelt, I.
Structural basis of proton-coupled potassium transport in the KUP family.
Nat Commun, 11:626-626, 2020

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/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.

PubMed: 32005818
DOI: 10.1038/s41467-020-14441-7

Experimental method

ELECTRON MICROSCOPY (3.7 Å)