Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2051280 | FEBS Letters | 2007 | 4 Pages |
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′-(β,γ-imido)triphosphate (AMP-PNP) at 3.4 Å 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.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Roger J.P. Dawson, Kaspar P. Locher,