2HYD
Multidrug ABC transporter SAV1866
2HYD の概要
| エントリーDOI | 10.2210/pdb2hyd/pdb |
| 分子名称 | ABC transporter homolog, SODIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| 機能のキーワード | transport protein |
| 由来する生物種 | Staphylococcus aureus |
| 細胞内の位置 | Cell membrane; Multi-pass membrane protein: Q99T13 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 130768.31 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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