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FEBS Lett. 2007 Mar 6;581(5):935-8. Epub 2007 Feb 7.

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

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1
Institute of Molecular Biology and Biophysics, ETH Zurich HPK D14.3, 8093 Zurich, Switzerland.

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.

PMID:
17303126
DOI:
10.1016/j.febslet.2007.01.073
[Indexed for MEDLINE]
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