| Structural highlights
4aux is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Related: | 1a6i, 1bj0, 1bjy, 1bjz, 1du7, 1ork, 1qpi, 2tct, 2trt, 2vke, 2vkv, 2x6o, 2x9d, 2xb5, 2xgc, 2xgd, 2xge, 2xps, 2xpt, 2xpu, 2xpv, 2xpw, 2xrl, 3zqf, 3zqg, 3zqh, 3zqi, 4abz |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
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.
Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance.,Hinrichs W, Kisker C, Duvel M, Muller A, Tovar K, Hillen W, Saenger W Science. 1994 Apr 15;264(5157):418-20. PMID:8153629[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. 1994 Apr 15;264(5157):418-20. PMID:8153629
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