7N9K

KirBac3.1 L124M mutant

7N9K の概要

• エントリーDOI: 10.2210/pdb7n9k/pdb
• 分子名称: Inward rectifier potassium channel Kirbac3.1, 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, trimethylamine oxide, ... (6 entities in total)
• 機能のキーワード: potassium channel gating, mutant, membrane protein
• 由来する生物種: Magnetospirillum magnetotacticum (Aquaspirillum magnetotacticum)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36593.06

構造登録者

Black, T.A.,Gulbis, J.M. (登録日: 2021-06-18, 公開日: 2021-12-29, 最終更新日: 2023-10-18)

主引用文献

Jin, R.,He, S.,Black, K.A.,Clarke, O.B.,Wu, D.,Bolla, J.R.,Johnson, P.,Periasamy, A.,Wardak, A.,Czabotar, P.,Colman, P.M.,Robinson, C.V.,Laver, D.,Smith, B.J.,Gulbis, J.M.
Ion currents through Kir potassium channels are gated by anionic lipids.
Nat Commun, 13:490-490, 2022

PubMed Abstract: Ion currents through potassium channels are gated. Constriction of the ion conduction pathway at the inner helix bundle, the textbook gate of Kir potassium channels, has been shown to be an ineffective permeation control, creating a rift in our understanding of how these channels are gated. Here we present evidence that anionic lipids act as interactive response elements sufficient to gate potassium conduction. We demonstrate the limiting barrier to K permeation lies within the ion conduction pathway and show that this gate is operated by the fatty acyl tails of lipids that infiltrate the conduction pathway via fenestrations in the walls of the pore. Acyl tails occupying a surface groove extending from the cytosolic interface to the conduction pathway provide a potential means of relaying cellular signals, mediated by anionic lipid head groups bound at the canonical lipid binding site, to the internal gate.

PubMed: 35079013
DOI: 10.1038/s41467-022-28148-4

実験手法

X-RAY DIFFRACTION (2.72 Å)