6S3K

KimA from Bacillus subtilis in inward-facing, occluded state

6S3K の概要

• エントリーDOI: 10.2210/pdb6s3k/pdb
• EMDBエントリー: 10092
• 分子名称: APC family permease, POTASSIUM ION (2 entities in total)
• 機能のキーワード: potassium transporter, leut fold, symporter, smalp, transport protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 133912.54

構造登録者

Tascon, I.,Sousa, J.S.,Vonck, J.,Haenelt, I. (登録日: 2019-06-25, 公開日: 2020-02-12, 最終更新日: 2025-07-02)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3.7 Å)