Molecular mechanism of proton-coupled ligand translocation by the bacterial efflux pump EmrE.

ABSTRACT: The current surge in bacterial multi-drug resistance (MDR) is one of the largest challenges to public health, threatening to render ineffective many therapies we rely on for treatment of serious infections. Understanding different factors that contribute to MDR is hence crucial from the global "one health" perspective. In this contribution, we focus on the prototypical broad-selectivity proton-coupled antiporter EmrE, one of the smallest known ligand transporters that confers resistance to aromatic cations in a number of clinically relevant species. As an asymmetric homodimer undergoing an "alternating access" protomer-swap conformational change, it serves as a model for the mechanistic understanding of more complex drug transporters. Here, we present a free energy and solvent accessibilit

SUBMITTER: Jurasz J 

PROVIDER: S-EPMC8523053 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature