7QEV

human Connexin 26 at 55mm Hg PCO2, pH7.4:two masked subunits, class D

7QEV の概要

• エントリーDOI: 10.2210/pdb7qev/pdb
• EMDBエントリー: 13942
• 分子名称: Gap junction beta-2 protein, DODECYL-BETA-D-MALTOSIDE, PHOSPHATIDYLETHANOLAMINE, ... (4 entities in total)
• 機能のキーワード: gap junction, ion channel, carbon dioxide sensitive, membrane protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57959.12

構造登録者

Brotherton, D.H.,Cameron, A.D.,Savva, C.G.,Ragan, T.J. (登録日: 2021-12-03, 公開日: 2022-06-15, 最終更新日: 2024-10-09)

主引用文献

Brotherton, D.H.,Savva, C.G.,Ragan, T.J.,Dale, N.,Cameron, A.D.
Conformational changes and CO 2 -induced channel gating in connexin26.
Structure, 30:697-706.e4, 2022

PubMed Abstract: Connexins form large-pore channels that function either as dodecameric gap junctions or hexameric hemichannels to allow the regulated movement of small molecules and ions across cell membranes. Opening or closing of the channels is controlled by a variety of stimuli, and dysregulation leads to multiple diseases. An increase in the partial pressure of carbon dioxide (PCO) has been shown to cause connexin26 (Cx26) gap junctions to close. Here, we use cryoelectron microscopy (cryo-EM) to determine the structure of human Cx26 gap junctions under increasing levels of PCO. We show a correlation between the level of PCO and the size of the aperture of the pore, governed by the N-terminal helices that line the pore. This indicates that CO alone is sufficient to cause conformational changes in the protein. Analysis of the conformational states shows that movements at the N terminus are linked to both subunit rotation and flexing of the transmembrane helices.

PubMed: 35276081
DOI: 10.1016/j.str.2022.02.010

実験手法

ELECTRON MICROSCOPY (2.9 Å)