A phage repressor–operator complex at 7 Å resolution
- 1 August 1985
- journal article
- Published by Springer Nature in Nature
- Vol. 316 (6029) , 596-601
- https://doi.org/10.1038/316596a0
Abstract
The crystal structure of a complex between the DNA-binding domain of phage 434 repressor and a synthetic 434 operator shows that the protein, very similar in conformation to gamma repressor, binds to B-form DNA with the second alpha-helix of a helix-turn-helix motif lying in the major groove.Keywords
This publication has 21 references indexed in Scilit:
- Ethylation interference and X-ray crystallography identify similar interactions between 434 repressor and operatorNature, 1985
- Molecular basis of DNA sequence recognition by the catabolite gene activator protein: detailed inferences from three mutations that alter DNA sequence specificity.Proceedings of the National Academy of Sciences, 1984
- Model of specific complex between catabolite gene activator protein and B-DNA suggested by electrostatic complementarity.Proceedings of the National Academy of Sciences, 1984
- DNA-Binding ProteinsScience, 1983
- The molecular basis of DNA–protein recognition inferred from the structure of cro repressorNature, 1982
- Homology among DNA-binding proteins suggests use of a conserved super-secondary structureNature, 1982
- The operator-binding domain of λ repressor: structure and DNA recognitionNature, 1982
- Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins.Proceedings of the National Academy of Sciences, 1982
- Structure of the cro repressor from bacteriophage λ and its interaction with DNANature, 1981
- Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNANature, 1981