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- W1451302247 abstract "Multidrug and toxic compound extrusion (MATE) proteins constitute a ubiquitous family of multidrug transporters and couple the efflux of structurally dissimilar drugs to the influx of either Na+ or H+. The ~900 MATE transporters identified thus far can be classified into the NorM, DinF (DNA-damage-inducible protein F) and eukaryotic subfamilies based on amino-acid sequence similarity. Structures of Na+-coupled, extracellular-facing NorM transporters had been determined, which revealed twelve membrane-spanning segments that are related by a quasi-twofold rotational symmetry as well as a multidrug-binding cavity situated near the membrane-periplasm interface. Here we report the crystal structures of an H+-coupled MATE transporter from the DinF subfamily, with and without substrate, unveiling a surprisingly asymmetric arrangement of twelve transmembrane helices and a largely hydrophobic multidrug-binding chamber located in the middle of the lipid bilayer. Combining structural and biochemical analyses, we confirmed the biological relevance of the substrate-binding site and suggested a direct competition between H+ and substrate during DinF-mediated drug transport. Our findings provided fundamental brushstrokes to the molecular picture depicting how a MATE transporter works and laid the groundwork for future experimental efforts aimed at overcoming multidrug resistance." @default.
- W1451302247 created "2016-06-24" @default.
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- W1451302247 date "2015-04-01" @default.
- W1451302247 modified "2023-09-23" @default.
- W1451302247 title "Structure of an H + ‐coupled, Substrate‐bound MATE Transporter Yields Mechanistic Insights into Multidrug Extrusion" @default.
- W1451302247 doi "https://doi.org/10.1096/fasebj.29.1_supplement.574.2" @default.
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