Sodium and proton coupling in the conformational cycle of a MATE antiporter from Vibrio cholerae.

ABSTRACT: Secondary active transporters belonging to the multidrug and toxic compound extrusion (MATE) family harness the potential energy of electrochemical ion gradients to export a broad spectrum of cytotoxic compounds, thus contributing to multidrug resistance. The current mechanistic understanding of ion-coupled substrate transport has been informed by a limited set of MATE transporter crystal structures from multiple organisms that capture a 12-transmembrane helix topology adopting similar outward-facing conformations. Although these structures mapped conserved residues important for function, the mechanistic role of these residues in shaping the conformational cycle has not been investigated. Here, we use double-electron electron resonance (DEER) spectroscopy to explore ligand-dependent confo

SUBMITTER: Claxton DP 

PROVIDER: S-EPMC6142240 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature