6KFH

Undocked hemichannel of an N-terminal deletion mutant of INX-6 in a nanodisc

6KFH の概要

• エントリーDOI: 10.2210/pdb6kfh/pdb
• EMDBエントリー: 9973
• 分子名称: Innexin-6 (1 entity in total)
• 機能のキーワード: gap junctions, innexin, transport protein
• 由来する生物種: Caenorhabditis elegans
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 361390.13

構造登録者

Burendei, B.,Shinozaki, R.,Watanabe, M.,Terada, T.,Tani, K.,Fujiyoshi, Y.,Oshima, A. (登録日: 2019-07-07, 公開日: 2020-02-12, 最終更新日: 2020-03-11)

主引用文献

Burendei, B.,Shinozaki, R.,Watanabe, M.,Terada, T.,Tani, K.,Fujiyoshi, Y.,Oshima, A.
Cryo-EM structures of undocked innexin-6 hemichannels in phospholipids.
Sci Adv, 6:eaax3157-eaax3157, 2020

PubMed Abstract: Gap junctions form intercellular conduits with a large pore size whose closed and open states regulate communication between adjacent cells. The structural basis of the mechanism by which gap junctions close, however, remains uncertain. Here, we show the cryo-electron microscopy structures of innexin-6 (INX-6) gap junction proteins in an undocked hemichannel form. In the nanodisc-reconstituted structure of the wild-type INX-6 hemichannel, flat double-layer densities obstruct the channel pore. Comparison of the hemichannel structures of a wild-type INX-6 in detergent and nanodisc-reconstituted amino-terminal deletion mutant reveals that lipid-mediated amino-terminal rearrangement and pore obstruction occur upon nanodisc reconstitution. Together with molecular dynamics simulations and electrophysiology functional assays, our results provide insight into the closure of the INX-6 hemichannel in a lipid bilayer before docking of two hemichannels.

PubMed: 32095518
DOI: 10.1126/sciadv.aax3157

実験手法

ELECTRON MICROSCOPY (3.6 Å)