Crystal structures of bacterial small multidrug resistance transporter EmrE in complex with structurally diverse substrates.

ABSTRACT: Proteins from the bacterial small multidrug resistance (SMR) family are proton-coupled exporters of diverse antiseptics and antimicrobials, including polyaromatic cations and quaternary ammonium compounds. The transport mechanism of the Escherichia coli transporter, EmrE, has been studied extensively, but a lack of high-resolution structural information has impeded a structural description of its molecular mechanism. Here, we apply a novel approach, multipurpose crystallization chaperones, to solve several structures of EmrE, including a 2.9 Å structure at low pH without substrate. We report five additional structures in complex with structurally diverse transported substrates, including quaternary phosphonium, quaternary ammonium, and planar polyaromatic compounds. These structures

SUBMITTER: Kermani AA 

PROVIDER: S-EPMC9000954 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature