Fueling the MATE transporterby Liz Entman Jul. 20, 2018, 8:58 AM
Evolutionarily conserved transport proteins, such as those belonging to the multidrug and toxic compound extrusion (MATE) superfamily, protect cells against toxic chemicals and contribute to multidrug resistance in cancer and bacterial cells.
Understanding how such transporters harness the energy of ion gradients to facilitate drug export is critical in developing novel anti-cancer and anti-bacterial drugs that can overcome resistance.
Reporting last month in the Proceedings of the National Academy of Sciences, Hassane Mchaourab, PhD, and colleagues used DEER (double-electron electron resonance) spectroscopy to show how some conserved amino acid residues in NorM, a MATE transporter from the cholera pathogen, mediate the structural changes involved in drug efflux.