1OTU

Structure of the Escherichia coli ClC Chloride channel E148Q mutant and Fab Complex

1OTU の概要

• エントリーDOI: 10.2210/pdb1otu/pdb
• 関連するPDBエントリー: 1OTS 1OTT
• 分子名称: Voltage-gated ClC-type chloride channel eriC, Fab fragment (Heavy chain), Fab fragment (Light chain), ... (4 entities in total)
• 機能のキーワード: ion channel, clc chloride channel, fab complex, membrane protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein (Probable): P37019
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 193351.09

構造登録者

Dutzler, R.,Campbell, E.B.,MacKinnon, R. (登録日: 2003-03-23, 公開日: 2003-04-15, 最終更新日: 2023-08-16)

主引用文献

Dutzler, R.,Campbell, E.B.,MacKinnon, R.
Gating the Selectivity Filter in ClC Chloride Channels
Science, 300:108-112, 2003

PubMed Abstract: ClC channels conduct chloride (Cl-) ions across cell membranes and thereby govern the electrical activity of muscle cells and certain neurons, the transport of fluid and electrolytes across epithelia, and the acidification of intracellular vesicles. The structural basis of ClC channel gating was studied. Crystal structures of wild-type and mutant Escherichia coli ClC channels bound to a monoclonal Fab fragment reveal three Cl- binding sites within the 15-angstrom neck of an hourglass-shaped pore. The Cl- binding site nearest the extracellular solution can be occupied either by a Cl- ion or by a glutamate carboxyl group. Mutations of this glutamate residue in Torpedo ray ClC channels alter gating in electrophysiological assays. These findings reveal a form of gating in which the glutamate carboxyl group closes the pore by mimicking a Cl- ion.

PubMed: 12649487
DOI: 10.1126/science.1082708

実験手法

X-RAY DIFFRACTION (3.3 Å)