6ids

Publication Abstract from PubMed

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.

Structural Basis of H(+)-Dependent Conformational Change in a Bacterial MATE Transporter.,Kusakizako T, Claxton DP, Tanaka Y, Maturana AD, Kuroda T, Ishitani R, Mchaourab HS, Nureki O Structure. 2018 Oct 30. pii: S0969-2126(18)30365-4. doi:, 10.1016/j.str.2018.10.004. PMID:30449688^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.