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 PubMed
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.
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 Also
References
- ↑ Dawson RJ, Locher KP. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett. 2007 Mar 6;581(5):935-8. Epub 2007 Feb 7. PMID:17303126 doi:10.1016/j.febslet.2007.01.073
