2ONJ

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

Summary for 2ONJ

• Entry DOI: 10.2210/pdb2onj/pdb
• Descriptor: Multidrug export ATP-binding/permease protein SAV1866, SODIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• Functional Keywords: integral membrane protein, transport protein, hydrolase
• Biological source: Staphylococcus aureus
• Cellular location: Cell membrane; Multi-pass membrane protein: Q99T13
• Total number of polymer chains: 2
• Total formula weight: 130972.28

Authors

Dawson, R.J.P.,Locher, K.P. (deposition date: 2007-01-24, release date: 2007-03-13, Last modification date: 2023-12-27)

Primary citation

Dawson, R.J.P.,Locher, K.P.
Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP.
Febs Lett., 581:935-938, 2007

PubMed 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.

PubMed: 17303126
DOI: 10.1016/j.febslet.2007.01.073

Experimental method

X-RAY DIFFRACTION (3.4 Å)