Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC Cl^-/H⁺ antiporter.

ABSTRACT: The CLC family of proteins are involved in a variety of physiological processes to control cellular chloride concentration. Two distinct classes of CLC proteins, Cl^- channels and Cl^-/H⁺ antiporters, have been functionally and structurally investigated over the last several decades. Previous studies have suggested that the conformational heterogeneity of the critical glutamate residue, Glu_ex, could explain the transport cycle of CLC-type Cl^-/H⁺ antiporters. However, the presence of multiple conformations (Up, Middle, and Down) of the Glu_ex has been suggested from combined structural snapshots of 2 different CLC antiporters: CLC-ec1 from Escherichia coli and cmCLC from a thermophilic red

SUBMITTER: Park K 

PROVIDER: S-EPMC6717299 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature