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- W4254979504 abstract "Multidrug transporters of the ABC family facilitate the export of diverse cytotoxic drugs across cell membranes. This is clinically relevant, as tumour cells may become resistant to agents used in chemotherapy. To understand the molecular basis of this process, we have determined the 3.0 A crystal structure of a bacterial ABC transporter (Sav1866) from Staphylococcus aureus. The homodimeric protein consists of 12 transmembrane helices in an arrangement that is consistent with cross-linking studies and electron microscopic imaging of the human multidrug resistance protein MDR1, but critically different from that reported for the bacterial lipid flippase MsbA. The observed, outward-facing conformation reflects the ATP-bound state, with the two nucleotide-binding domains in close contact and the two transmembrane domains forming a central cavity--presumably the drug translocation pathway--that is shielded from the inner leaflet of the lipid bilayer and from the cytoplasm, but exposed to the outer leaflet and the extracellular space. PMID: 16943773" @default.
- W4254979504 created "2022-05-12" @default.
- W4254979504 creator A5024135496 @default.
- W4254979504 date "2006-09-15" @default.
- W4254979504 modified "2023-09-27" @default.
- W4254979504 title "Faculty Opinions recommendation of Structure of a bacterial multidrug ABC transporter." @default.
- W4254979504 doi "https://doi.org/10.3410/f.1040411.490926" @default.
- W4254979504 hasPublicationYear "2006" @default.
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