7N9K

KirBac3.1 L124M mutant

Summary for 7N9K

• Entry DOI: 10.2210/pdb7n9k/pdb
• Descriptor: Inward rectifier potassium channel Kirbac3.1, 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, trimethylamine oxide, ... (6 entities in total)
• Functional Keywords: potassium channel gating, mutant, membrane protein
• Biological source: Magnetospirillum magnetotacticum (Aquaspirillum magnetotacticum)
• Total number of polymer chains: 1
• Total formula weight: 36593.06

Authors

Black, T.A.,Gulbis, J.M. (deposition date: 2021-06-18, release date: 2021-12-29, Last modification date: 2023-10-18)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.72 Å)