Conserved binding site in the N-lobe of prokaryotic MATE transporters suggests a role for Na⁺ in ion-coupled drug efflux.

ABSTRACT: In both prokaryotes and eukaryotes, multidrug and toxic-compound extrusion (MATE) transporters catalyze the efflux of a broad range of cytotoxic compounds, including human-made antibiotics and anticancer drugs. MATEs are secondary-active antiporters, i.e., their drug-efflux activity is coupled to, and powered by, the uptake of ions down a preexisting transmembrane electrochemical gradient. Key aspects of this mechanism, however, remain to be delineated, such as its ion specificity and stoichiometry. We previously revealed the existence of a Na⁺-binding site in a MATE transporter from Pyroccocus furiosus (PfMATE) and hypothesized that this site might be broadly conserved among prokaryotic MATEs. Here, we evaluate this hypothesis by analyzing VcmN and ClbM, which along with PfMATE

SUBMITTER: Castellano S 

PROVIDER: S-EPMC7949106 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature