The role of conformational change and key glutamic acid residues in the ClC-ec1 antiporter.

ABSTRACT: The triple glutamine (Q) mutant (QQQ) structure of a Cl^-/H⁺ antiporter from Escherichia coli (ClC-ec1) displaying a novel backbone arrangement has been used to challenge the long-held notion that Cl^-/H⁺ antiporters do not operate through large conformational motions. The QQQ mutant substitutes the glutamine residue for an external glutamate E148, an internal glutamate E203, and a third glutamate E113 that hydrogen-bonds with E203. However, it is unknown if QQQ represents a physiologically relevant state, as well as how the protonation of the wild-type glutamates relates to the global dynamics. We herein apply continuous constant-pH molecular dynamics to investigate the H⁺-coupled dynamics of ClC-ec1. Although any large-scale conformati

SUBMITTER: Yue Z 

PROVIDER: S-EPMC10111279 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature