2EZ0

Crystal structure of the S107A/E148Q/Y445A mutant of EcClC, in complex with a FaB fragment

2EZ0 の概要

• エントリーDOI: 10.2210/pdb2ez0/pdb
• 関連するPDBエントリー: 1OTS 2exw 2exy
• 分子名称: H(+)/Cl(-) exchange transporter clcA, Fab Fragment (Heavy Chain), Fab Fragment (Light Chain), ... (4 entities in total)
• 機能のキーワード: clc family of channels and transporters, h+/cl- antiporter, membrane protein-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: 194545.40

構造登録者

Lobet, S.,Dutzler, R. (登録日: 2005-11-10, 公開日: 2006-01-24, 最終更新日: 2024-10-09)

主引用文献

Lobet, S.,Dutzler, R.
Ion-binding properties of the ClC chloride selectivity filter.
Embo J., 25:24-33, 2006

PubMed Abstract: The ClC channels are members of a large protein family of chloride (Cl-) channels and secondary active Cl- transporters. Despite their diverse functions, the transmembrane architecture within the family is conserved. Here we present a crystallographic study on the ion-binding properties of the ClC selectivity filter in the close homolog from Escherichia coli (EcClC). The ClC selectivity filter contains three ion-binding sites that bridge the extra- and intracellular solutions. The sites bind Cl- ions with mM affinity. Despite their close proximity within the filter, the three sites can be occupied simultaneously. The ion-binding properties are found conserved from the bacterial transporter EcClC to the human Cl- channel ClC-1, suggesting a close functional link between ion permeation in the channels and active transport in the transporters. In resemblance to K+ channels, ions permeate the ClC channel in a single file, with mutual repulsion between the ions fostering rapid conduction.

PubMed: 16341087
DOI: 10.1038/sj.emboj.7600909

実験手法

X-RAY DIFFRACTION (3.54 Å)