2onj | pdb_00002onj

Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP

spinqualitylabelsall models 2onj, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2onj is a 2 chain structure with sequence from Staphylococcus aureus. The November 2007 RCSB PDB Molecule of the Month feature on Multidrug Resistance Transporters by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4Å Ligands: ANP, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Y1866_STAAM May be involved in multidrug export. Transmembrane domains (TMD) form a pore in the cell membrane and the ATP-binding domain (NBD) is responsible for energy generation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Staphylococcus aureus Sav1866 is a bacterial homolog of the human ABC transporter Mdr1 that causes multidrug resistance in cancer cells. We report the crystal structure of Sav1866 in complex with adenosine-5'-(beta,gamma-imido)triphosphate (AMP-PNP) at 3.4A resolution and compare it with the previously determined structure of Sav1866 with bound ADP. Besides differences in the ATP-binding sites, no significant conformational changes were observed. The results confirm that the ATP-bound state of multidrug ABC transporters is coupled to an outward-facing conformation of the transmembrane domains. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP.,Dawson RJ, Locher KP FEBS Lett. 2007 Mar 6;581(5):935-8. Epub 2007 Feb 7. PMID:17303126 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter 3D structures

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