2OR1
RECOGNITION OF A DNA OPERATOR BY THE REPRESSOR OF PHAGE 434. A VIEW AT HIGH RESOLUTION
Summary for 2OR1
| Entry DOI | 10.2210/pdb2or1/pdb |
| Descriptor | DNA (5'-D(*AP*AP*GP*TP*AP*CP*AP*AP*AP*CP*TP*TP*TP*CP*TP*TP*G P*TP*AP*T)-3'), DNA (5'-D(*TP*AP*TP*AP*CP*AP*AP*GP*AP*AP*AP*GP*TP*TP*TP*GP*T P*AP*CP*T)-3'), 434 REPRESSOR, ... (4 entities in total) |
| Functional Keywords | protein-dna complex, double helix, gene regulation-dna complex, gene regulation/dna |
| Biological source | Phage 434 |
| Total number of polymer chains | 4 |
| Total formula weight | 27384.10 |
| Authors | Aggarwal, A.K.,Rodgers, D.W.,Drottar, M.,Ptashne, M.,Harrison, S.C. (deposition date: 1989-09-05, release date: 1989-09-05, Last modification date: 2024-02-21) |
| Primary citation | Aggarwal, A.K.,Rodgers, D.W.,Drottar, M.,Ptashne, M.,Harrison, S.C. Recognition of a DNA operator by the repressor of phage 434: a view at high resolution. Science, 242:899-907, 1988 Cited by PubMed Abstract: The repressors of temperate bacteriophages such as 434 and lambda control transcription by binding to a set of DNA operator sites. The different affinity of repressor for each of these sites ensures efficient regulation. High-resolution x-ray crystallography was used to study the DNA-binding domain of phage 434 repressor in complex with a synthetic DNA operator. The structure shows recognition of the operator by direct interactions with base pairs in the major groove, combined with the sequence-dependent ability of DNA to adopt the required conformation on binding repressor. In particular, a network of three-centered bifurcated hydrogen bonds among base pairs in the operator helps explain why 434 repressor prefers certain sites over others. These bonds, which stabilize the conformation of the bound DNA, can form only with certain sequences. PubMed: 3187531PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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