The C terminus of the bacterial multidrug transporter EmrE couples drug binding to proton release.

ABSTRACT: Ion-coupled transporters must regulate access of ions and substrates into and out of the binding site to actively transport substrates and minimize dissipative leak of ions. Within the single-site alternating access model, competitive substrate binding forms the foundation of ion-coupled antiport. Strict competition between substrates leads to stoichiometric antiport without slippage. However, recent NMR studies of the bacterial multidrug transporter EmrE have demonstrated that this multidrug transporter can simultaneously bind drug and proton, which will affect the transport stoichiometry and efficiency of coupled antiport. Here, we investigated the nature of substrate competition in EmrE using multiple methods to measure proton release upon the addition of saturating concentrations of dr

SUBMITTER: Thomas NE 

PROVIDER: S-EPMC6295725 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature