1JUS
Crystal structure of the multidrug binding transcriptional repressor QacR bound to rhodamine 6G
Summary for 1JUS
| Entry DOI | 10.2210/pdb1jus/pdb |
| Related | 1JT0 1JT6 1JTX 1JTY 1JUM 1JUP |
| Descriptor | HYPOTHETICAL TRANSCRIPTIONAL REGULATOR IN QACA 5'REGION, SULFATE ION, RHODAMINE 6G, ... (4 entities in total) |
| Functional Keywords | multidrug recognition, s. aureus, qacr, rhodamine 6g, cationic lipophilic drugs, transcription |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 4 |
| Total formula weight | 95147.83 |
| Authors | Schumacher, M.A.,Miller, M.C.,Grkovic, S.,Brown, M.H.,Skurray, R.A.,Brennan, R.G. (deposition date: 2001-08-27, release date: 2001-12-12, Last modification date: 2024-11-20) |
| Primary citation | Schumacher, M.A.,Miller, M.C.,Grkovic, S.,Brown, M.H.,Skurray, R.A.,Brennan, R.G. Structural mechanisms of QacR induction and multidrug recognition. Science, 294:2158-2163, 2001 Cited by PubMed Abstract: The Staphylococcus aureus multidrug binding protein QacR represses transcription of the qacA multidrug transporter gene and is induced by structurally diverse cationic lipophilic drugs. Here, we report the crystal structures of six QacR-drug complexes. Compared to the DNA bound structure, drug binding elicits a coil-to-helix transition that causes induction and creates an expansive multidrug-binding pocket, containing four glutamates and multiple aromatic and polar residues. These structures indicate the presence of separate but linked drug-binding sites within a single protein. This multisite drug-binding mechanism is consonant with studies on multidrug resistance transporters. PubMed: 11739955DOI: 10.1126/science.1066020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.84 Å) |
Structure validation
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