4WLS
Crystal structure of the metal-free (repressor) form of E. Coli CUER, a copper efflux regulator, bound to COPA promoter DNA
Summary for 4WLS
| Entry DOI | 10.2210/pdb4wls/pdb |
| Related | 4WLW |
| Descriptor | HTH-type transcriptional regulator CueR, COPA PROMOTER DNA NON-TEMPLATE STRAND, COPA PROMOTER DNA TEMPLATE STRAND, ... (6 entities in total) |
| Functional Keywords | protein-dna complex, merr-family transcription regulator, metal-free form, repressor, transcription, transcription regulator-dna complex, transcription regulator/dna |
| Biological source | Escherichia coli DH5[alpha] More |
| Total number of polymer chains | 6 |
| Total formula weight | 61144.28 |
| Authors | Philips, S.J.,Canalizo-Hernandez, M.,Mondragon, A.,O'Halloran, T.V. (deposition date: 2014-10-08, release date: 2015-09-02, Last modification date: 2024-10-30) |
| Primary citation | Philips, S.J.,Canalizo-Hernandez, M.,Yildirim, I.,Schatz, G.C.,Mondragon, A.,O'Halloran, T.V. Allosteric transcriptional regulation via changes in the overall topology of the core promoter. Science, 349:877-881, 2015 Cited by PubMed Abstract: Many transcriptional activators act at a distance from core promoter elements and work by recruiting RNA polymerase through protein-protein interactions. We show here how the prokaryotic regulatory protein CueR both represses and activates transcription by differentially modulating local DNA structure within the promoter. Structural studies reveal that the repressor state slightly bends the promoter DNA, precluding optimal RNA polymerase-promoter recognition. Upon binding a metal ion in the allosteric site, CueR switches into an activator conformation. It maintains all protein-DNA contacts but introduces torsional stresses that kink and undertwist the promoter, stabilizing an A-form DNA-like conformation. These factors switch on and off transcription by exerting dynamic control of DNA stereochemistry, reshaping the core promoter and making it a better or worse substrate for polymerase. PubMed: 26293965DOI: 10.1126/science.aaa9809 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.105 Å) |
Structure validation
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