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Abstract

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.

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PubMed ID:: 17303126

DOI:: 10.1016/j.febslet.2007.01.073

ScienceOpen disciplines: Chemistry

Keywords: ATP-Binding Cassette Transporters,chemistry,genetics,metabolism,Adenosine Triphosphatases,Adenylyl Imidodiphosphate,Bacterial Proteins,Crystallography, X-Ray,Drug Stability,Models, Molecular,Protein Binding,Protein Conformation,Recombinant Proteins,Staphylococcus aureus

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ScienceOpen disciplines: Chemistry

Keywords: ATP-Binding Cassette Transporters, chemistry, genetics, metabolism, Adenosine Triphosphatases, Adenylyl Imidodiphosphate, Bacterial Proteins, Crystallography, X-Ray, Drug Stability, Models, Molecular, Protein Binding, Protein Conformation, Recombinant Proteins, Staphylococcus aureus

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