2XPU
TetR(D) in complex with anhydrotetracycline.
Summary for 2XPU
| Entry DOI | 10.2210/pdb2xpu/pdb |
| Related | 1A6I 1BJ0 1BJY 1BJZ 1DU7 1ORK 1QPI 2TCT 2TRT 2VKE 2VKV 2X6O 2X9D 2XB5 2XGC 2XGD 2XGE 2XPS 2XPT 2XPV 2XPW 2XRL 3ZQF 3ZQG 3ZQH 3ZQI |
| Descriptor | TETRACYCLINE REPRESSOR PROTEIN CLASS D, 5A,6-ANHYDROTETRACYCLINE, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | transcription, transcription regulator, helix-turn-helix, metal coordination |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 1 |
| Total formula weight | 23881.72 |
| Authors | Dalm, D.,Palm, G.J.,Hinrichs, W. (deposition date: 2010-08-30, release date: 2011-09-07, Last modification date: 2023-12-20) |
| Primary citation | Werten, S.,Dalm, D.,Palm, G.J.,Grimm, C.C.,Hinrichs, W. Tetracycline Repressor Allostery Does not Depend on Divalent Metal Recognition. Biochemistry, 53:7990-, 2014 Cited by PubMed Abstract: Genes that render bacteria resistant to tetracycline-derived antibiotics are tightly regulated by repressors of the TetR family. In their physiologically relevant, magnesium-complexed form, tetracyclines induce allosteric rearrangements in the TetR homodimer, leading to its release from the promoter and derepression of transcription. According to earlier crystallographic work, recognition of the tetracycline-associated magnesium ion by TetR is crucial and triggers the allosteric cascade. Nevertheless, the derivative 5a,6-anhydrotetracycline, which shows an increased affinity for TetR, causes promoter release even in the absence of magnesium. To resolve this paradox, it has been proposed that metal-free 5a,6-anhydrotetracycline acts via an exceptional, conformationally different induction mode that circumvents the normal magnesium requirement. We have tested this hypothesis by determining crystal structures of TetR-5a,6-anhydrotetracycline complexes in the presence of magnesium, ethylenediaminetetraacetic acid, or high concentrations of potassium. Analysis of these three structures reveals that, irrespective of the metal, the effects of 5a,6-anhydrotetracycline binding are indistinguishable from those of canonical induction by other tetracyclines. Together with a close scrutiny of the earlier evidence of a metal-triggered mechanism, these results demonstrate that magnesium recognition per se is not a prerequisite for tetracycline repressor allostery. PubMed: 25432019DOI: 10.1021/BI5012805 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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