2onj | pdb_00002onj
From Proteopedia
Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP
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Structural highlights
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 PubMedStaphylococcus 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 07:52, 2 March 2022.