1RIO
Structure of bacteriophage lambda cI-NTD in complex with sigma-region4 of Thermus aquaticus bound to DNA
Summary for 1RIO
| Entry DOI | 10.2210/pdb1rio/pdb |
| Related | 1KU7 1LMB |
| Descriptor | 27-MER, sigma factor SigA, Repressor protein CI, ... (7 entities in total) |
| Functional Keywords | helix-turn-helix, transcription activation, transcription-dna complex, transcription/dna |
| Biological source | Thermus aquaticus More |
| Total number of polymer chains | 5 |
| Total formula weight | 47773.62 |
| Authors | Jain, D.,Nickels, B.E.,Sun, L.,Hochschild, A.,Darst, S.A. (deposition date: 2003-11-17, release date: 2004-01-27, Last modification date: 2024-11-20) |
| Primary citation | Jain, D.,Nickels, B.E.,Sun, L.,Hochschild, A.,Darst, S.A. Structure of a ternary transcription activation complex. Mol.Cell, 13:45-53, 2004 Cited by PubMed Abstract: The cI protein of bacteriophage lambda (lambdacI) activates transcription by binding a DNA operator just upstream of the promoter and interacting with the RNA polymerase sigma subunit domain 4 (sigma(4)). We determined the crystal structure of the lambdacI/sigma(4)/DNA ternary complex at 2.3 A resolution. There are no conformational changes in either protein, which interact through an extremely small interface involving at most 6 amino acid residues. The interactions of the two proteins stabilize the binding of each protein to the DNA. The results provide insight into how activators can operate through a simple cooperative binding mechanism but affect different steps of the transcription initiation process. PubMed: 14731393DOI: 10.1016/S1097-2765(03)00483-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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