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- W3138375724 abstract "Abstract Multidrug ABC transporters translocate drugs across membranes by a mechanism for which the molecular features of drug release are so far unknown. Here, we resolved two ATP-Mg 2+ -bound outward-facing (OF) conformations of the Bacillus subtilis (homodimeric) BmrA, one by X-ray crystallography without drug, and another by single-particle cryo-EM with rhodamine 6G (R6G). Two R6G molecules bind to the drug-binding cavity at the level of the outer leaflet, between transmembrane (TM) helices 1-2 of one monomer and TM5’-6’ of the other. R6G induces a rearrangement of TM1-2, highlighting a flexibility that was confirmed by H/D exchange and molecular dynamics simulations. The latter also shows a fast post-release occlusion of the cavity driven by hydrophobicity. Altogether, these data support a new swing mechanism for drug transport." @default.
- W3138375724 created "2021-03-29" @default.
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- W3138375724 date "2021-03-12" @default.
- W3138375724 modified "2023-10-16" @default.
- W3138375724 title "Drug-bound and -free outward-facing structures of a multidrug ABC exporter point to a swing mechanism" @default.
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- W3138375724 doi "https://doi.org/10.1101/2021.03.12.435132" @default.
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