Structural Basis of H⁺-Dependent Conformational Change in a Bacterial MATE Transporter.

ABSTRACT: Multidrug and toxic compound extrusion (MATE) transporters efflux toxic compounds using a Na⁺ or H⁺ gradient across the membrane. Although the structures of MATE transporters have been reported, the cation-coupled substrate transport mechanism remains controversial. Here we report crystal structures of VcmN, a Vibrio cholerae MATE transporter driven by the H⁺ gradient. High-resolution structures in two distinct conformations associated with different pHs revealed that the rearrangement of the hydrogen-bonding network around the conserved Asp35 induces the bending of transmembrane helix 1, as in the case of the H⁺-coupled Pyrococcus furiosus MATE transporter. We also determined the crystal structure of the D35N mutant, which captured a unique conformation of TM1 facilitated by an altered hydrogen-bonding network. Based on the present results, we propose a common step in the transport cycle shared among prokaryotic H⁺-coupled MATE transporters.

SUBMITTER: Kusakizako T 

PROVIDER: S-EPMC7935464 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature