2hyd
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(New page: 200px<br /><applet load="2hyd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hyd, resolution 3.0Å" /> '''Multidrug ABC transpo...)
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Revision as of 09:56, 21 November 2007
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Multidrug ABC transporter SAV1866
Overview
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.
About this Structure
2HYD is a Single protein structure of sequence from Staphylococcus aureus with NA and ADP as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a bacterial multidrug ABC transporter., Dawson RJ, Locher KP, Nature. 2006 Sep 14;443(7108):180-5. Epub 2006 Aug 30. PMID:16943773
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