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.