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 Cited by 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: 17303126DOI: 10.1016/j.febslet.2007.01.073 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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