1KPK

Crystal Structure of the ClC Chloride Channel from E. coli

1KPK の概要

• エントリーDOI: 10.2210/pdb1kpk/pdb
• 関連するPDBエントリー: 1KPL
• 分子名称: putative channel transporter (1 entity in total)
• 機能のキーワード: helical membrane protein, homodimer, membrane protein
• 由来する生物種: Escherichia coli
• 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: 302342.41

構造登録者

Dutzler, R.,Campbell, E.B.,Cadene, M.,Chait, B.T.,MacKinnon, R. (登録日: 2001-12-31, 公開日: 2002-01-23, 最終更新日: 2024-02-14)

主引用文献

Dutzler, R.,Campbell, E.B.,Cadene, M.,Chait, B.T.,MacKinnon, R.
X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity.
Nature, 415:287-294, 2002

PubMed Abstract: The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. Genetic defects in ClC Cl- channels underlie several familial muscle and kidney diseases. Here we present the X-ray structures of two prokaryotic ClC Cl- channels from Salmonella enterica serovar typhimurium and Escherichia coli at 3.0 and 3.5 A, respectively. Both structures reveal two identical pores, each pore being formed by a separate subunit contained within a homodimeric membrane protein. Individual subunits are composed of two roughly repeated halves that span the membrane with opposite orientations. This antiparallel architecture defines a selectivity filter in which a Cl- ion is stabilized by electrostatic interactions with alpha-helix dipoles and by chemical coordination with nitrogen atoms and hydroxyl groups. These findings provide a structural basis for further understanding the function of ClC Cl- channels, and establish the physical and chemical basis of their anion selectivity.

PubMed: 11796999
DOI: 10.1038/415287a

実験手法

X-RAY DIFFRACTION (3.5 Å)