6V2J

Crystal structure of ClC-ec1 triple mutant (E113Q, E148Q, E203Q)

6V2J の概要

• エントリーDOI: 10.2210/pdb6v2j/pdb
• 分子名称: H(+)/Cl(-) exchange transporter ClcA, CHLORIDE ION (3 entities in total)
• 機能のキーワード: chloride transporters, clc-ec1, transport protein
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52218.76

構造登録者

Maduke, M.,Mathews, I.I.,Chavan, T.S. (登録日: 2019-11-24, 公開日: 2020-05-20, 最終更新日: 2023-10-11)

主引用文献

Chavan, T.S.,Cheng, R.C.,Jiang, T.,Mathews, I.I.,Stein, R.A.,Koehl, A.,Mchaourab, H.S.,Tajkhorshid, E.,Maduke, M.
A CLC-ec1 mutant reveals global conformational change and suggests a unifying mechanism for the CLC Cl - /H + transport cycle.
Elife, 9:-, 2020

PubMed Abstract: Among coupled exchangers, CLCs uniquely catalyze the exchange of oppositely charged ions (Cl for H). Transport-cycle models to describe and explain this unusual mechanism have been proposed based on known CLC structures. While the proposed models harmonize with many experimental findings, gaps and inconsistencies in our understanding have remained. One limitation has been that global conformational change - which occurs in all conventional transporter mechanisms - has not been observed in any high-resolution structure. Here, we describe the 2.6 Å structure of a CLC mutant designed to mimic the fully H-loaded transporter. This structure reveals a global conformational change to improve accessibility for the Cl substrate from the extracellular side and new conformations for two key glutamate residues. Together with DEER measurements, MD simulations, and functional studies, this new structure provides evidence for a unified model of H/Cl transport that reconciles existing data on all CLC-type proteins.

PubMed: 32310757
DOI: 10.7554/eLife.53479

実験手法

X-RAY DIFFRACTION (2.62 Å)