Summary for 2TRT
| Entry DOI | 10.2210/pdb2trt/pdb |
| Descriptor | TETRACYCLINE REPRESSOR CLASS D, MAGNESIUM ION, TETRACYCLINE, ... (4 entities in total) |
| Functional Keywords | transcription regulation, repressor, dna-binding |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 24786.35 |
| Authors | Hinrichs, W.,Kisker, C.,Saenger, W. (deposition date: 1994-03-04, release date: 1996-06-20, Last modification date: 2024-02-21) |
| Primary citation | Hinrichs, W.,Kisker, C.,Duvel, M.,Muller, A.,Tovar, K.,Hillen, W.,Saenger, W. Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance. Science, 264:418-420, 1994 Cited by PubMed Abstract: The most frequently occurring resistance of Gram-negative bacteria against tetracyclines is triggered by drug recognition of the Tet repressor. This causes dissociation of the repressor-operator DNA complex and enables expression of the resistance protein TetA, which is responsible for active efflux of tetracycline. The 2.5 angstrom resolution crystal structure of the homodimeric Tet repressor complexed with tetracycline-magnesium reveals detailed drug recognition. The orientation of the operator-binding helix-turn-helix motifs of the repressor is inverted in comparison with other DNA binding proteins. The repressor-drug complex is unable to interact with DNA because the separation of the DNA binding motifs is 5 angstroms wider than usually observed. PubMed: 8153629PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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