2HYD
Multidrug ABC transporter SAV1866
Summary for 2HYD
| Entry DOI | 10.2210/pdb2hyd/pdb |
| Descriptor | ABC transporter homolog, SODIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | transport protein |
| Biological source | Staphylococcus aureus |
| Cellular location | Cell membrane; Multi-pass membrane protein: Q99T13 |
| Total number of polymer chains | 2 |
| Total formula weight | 130768.31 |
| Authors | Dawson, R.J.P.,Locher, K.P. (deposition date: 2006-08-05, release date: 2006-09-05, Last modification date: 2024-02-21) |
| Primary citation | Dawson, R.J.,Locher, K.P. Structure of a bacterial multidrug ABC transporter. Nature, 443:180-185, 2006 Cited by PubMed Abstract: Multidrug transporters of the ABC family facilitate the export of diverse cytotoxic drugs across cell membranes. This is clinically relevant, as tumour cells may become resistant to agents used in chemotherapy. To understand the molecular basis of this process, we have determined the 3.0 A crystal structure of a bacterial ABC transporter (Sav1866) from Staphylococcus aureus. The homodimeric protein consists of 12 transmembrane helices in an arrangement that is consistent with cross-linking studies and electron microscopic imaging of the human multidrug resistance protein MDR1, but critically different from that reported for the bacterial lipid flippase MsbA. The observed, outward-facing conformation reflects the ATP-bound state, with the two nucleotide-binding domains in close contact and the two transmembrane domains forming a central cavity--presumably the drug translocation pathway--that is shielded from the inner leaflet of the lipid bilayer and from the cytoplasm, but exposed to the outer leaflet and the extracellular space. PubMed: 16943773DOI: 10.1038/nature05155 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report
