3K33
Crystal structure of the Phd-Doc complex
Summary for 3K33
| Entry DOI | 10.2210/pdb3k33/pdb |
| Related | 3DD7 3HRY 3HS2 |
| Descriptor | Death on curing protein, Prevent host death protein, Polypeptide of unknown amino acids and source, ... (5 entities in total) |
| Functional Keywords | phd, doc, fic, toxin, antitoxin, intrinsic disorder, allostery, transcription regulation, ribosome inhibitor, toxin-antitoxin complex, toxin/antitoxin |
| Biological source | Enterobacteria phage P1 (Bacteriophage P1) More |
| Total number of polymer chains | 5 |
| Total formula weight | 39189.84 |
| Authors | Loris, R.,Garcia-Pino, A. (deposition date: 2009-10-01, release date: 2010-08-18, Last modification date: 2023-09-06) |
| Primary citation | Garcia-Pino, A.,Balasubramanian, S.,Wyns, L.,Gazit, E.,De Greve, H.,Magnuson, R.D.,Charlier, D.,van Nuland, N.A.,Loris, R. Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. Cell(Cambridge,Mass.), 142:101-111, 2010 Cited by PubMed Abstract: Regulation of the phd/doc toxin-antitoxin operon involves the toxin Doc as co- or derepressor depending on the ratio between Phd and Doc, a phenomenon known as conditional cooperativity. The mechanism underlying this observed behavior is not understood. Here we show that monomeric Doc engages two Phd dimers on two unrelated binding sites. The binding of Doc to the intrinsically disordered C-terminal domain of Phd structures its N-terminal DNA-binding domain, illustrating allosteric coupling between highly disordered and highly unstable domains. This allosteric effect also couples Doc neutralization to the conditional regulation of transcription. In this way, higher levels of Doc tighten repression up to a point where the accumulation of toxin triggers the production of Phd to counteract its action. Our experiments provide the basis for understanding the mechanism of conditional cooperative regulation of transcription typical of toxin-antitoxin modules. This model may be applicable for the regulation of other biological systems. PubMed: 20603017DOI: 10.1016/j.cell.2010.05.039 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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