4MQX

CLC-ec1 Fab Complex Cysless A399C-A432C mutant

4MQX の概要

• エントリーDOI: 10.2210/pdb4mqx/pdb
• 関連するPDBエントリー: 1OTS
• 分子名称: H(+)/Cl(-) exchange transporter ClcA, ecCLC, ERIC, ... (4 entities in total)
• 機能のキーワード: alpha helical transmembrane protein, cl/h antiporter, metal transport, 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: 193250.02

構造登録者

Basilio, D.,Noack, K.,Picollo, A.,Accardi, A. (登録日: 2013-09-16, 公開日: 2014-04-16, 最終更新日: 2024-11-27)

主引用文献

Basilio, D.,Noack, K.,Picollo, A.,Accardi, A.
Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter.
Nat.Struct.Mol.Biol., 21:456-463, 2014

PubMed Abstract: CLC-type exchangers mediate transmembrane Cl(-) transport. Mutations altering their gating properties cause numerous genetic disorders. However, their transport mechanism remains poorly understood. In conventional models, two gates alternatively expose substrates to the intra- or extracellular solutions. A glutamate was identified as the only gate in the CLCs, suggesting that CLCs function by a nonconventional mechanism. Here we show that transport in CLC-ec1, a prokaryotic homolog, is inhibited by cross-links constraining movement of helix O far from the transport pathway. Cross-linked CLC-ec1 adopts a wild-type-like structure, indicating stabilization of a native conformation. Movements of helix O are transduced to the ion pathway via a direct contact between its C terminus and a tyrosine that is a constitutive element of the second gate of CLC transporters. Therefore, the CLC exchangers have two gates that are coupled through conformational rearrangements outside the ion pathway.

PubMed: 24747941
DOI: 10.1038/nsmb.2814

実験手法

X-RAY DIFFRACTION (3.516 Å)