6FTS
TETR(D) N82A MUTANT IN COMPLEX WITH PEG4
Summary for 6FTS
| Entry DOI | 10.2210/pdb6fts/pdb |
| Related | 5FKK |
| Descriptor | Tetracycline repressor protein class D, TETRAETHYLENE GLYCOL, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | transcription regulation, transcription |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 23510.44 |
| Authors | Hinrichs, W.,Palm, G.J.,Berndt, L.,Girbardt, B. (deposition date: 2018-02-23, release date: 2019-02-20, Last modification date: 2024-01-17) |
| Primary citation | Palm, G.J.,Buchholz, I.,Werten, S.,Girbardt, B.,Berndt, L.,Delcea, M.,Hinrichs, W. Thermodynamics, cooperativity and stability of the tetracycline repressor (TetR) upon tetracycline binding. Biochim Biophys Acta Proteins Proteom, 1868:140404-140404, 2020 Cited by PubMed Abstract: Allosteric regulation of the Tet repressor (TetR) homodimer relies on tetracycline binding that abolishes the affinity for the DNA operator. Previously, interpretation of circular dichroism data called for unfolding of the α-helical DNA-binding domains in absence of binding to DNA or tetracycline. Our small angle X-ray scattering of TetR(D) in solution contradicts this unfolding as a physiological process. Instead, in the core domain crystal structures analyses show increased immobilisation of helix α9 and two C-terminal turns of helix α8 upon tetracycline binding. Tetracycline complexes of TetR(D) and four single-site alanine variants were characterised by isothermal titration calorimetry, fluorescence titration, X-ray crystal structures, and melting curves. Five crystal structures confirm that Thr103 is a key residue for the allosteric events of induction, with the T103A variant lacking induction by any tetracycline. The T103A variant shows anti-cooperative inducer binding, and a melting curve of the tetracycline complex different to TetR(D) and other variants. For the N82A variant inducer binding is clearly anti-cooperative but triggers the induced conformation. PubMed: 32114262DOI: 10.1016/j.bbapap.2020.140404 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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