Summary information and primary citation
- PDB-id
- 1rio; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- transcription-DNA
- Method
- X-ray (2.3 Å)
- Summary
- Structure of bacteriophage lambda ci-ntd in complex with sigma-region4 of thermus aquaticus bound to DNA
- Reference
- Jain D, Nickels BE, Sun L, Hochschild A, Darst SA (2004): "Structure of a ternary transcription activation complex." Mol.Cell, 13, 45-53. doi: 10.1016/S1097-2765(03)00483-0.
- 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.
