Structure of the cro repressor from bacteriophage λ and its interaction with DNA
- 1 April 1981
- journal article
- Published by Springer Nature in Nature
- Vol. 290 (5809) , 754-758
- https://doi.org/10.1038/290754a0
Abstract
The three-dimensional structure of the 66-amino acid cro repressor protein of bacteriophage lambda suggests how it binds to its operator DNA. We propose that a dimer of cro protein is bound to the B-form of DNA with the 2-fold axis of the dimer coincident with the 2-fold axis of DNA. A pair of 2-fold-related alpha-helices of the repressor, lying within successive major grooves of the DNA, seem to be a major determinant in recognition and binding. In addition, the C-terminal residues of the protein, some of which are disordered in the absence of DNA, appear to contribute to the binding.Keywords
This publication has 27 references indexed in Scilit:
- How the λ repressor and cro workCell, 1980
- Specific repression of in vitro transcription by the Cro repressor of bacteriophage lambdaJournal of Molecular Biology, 1979
- Mechanism of action of the cro protein of bacteriophage lambda.Proceedings of the National Academy of Sciences, 1978
- Amino acid sequence of Cro regulatory protein of bacteriophage lambdaNature, 1977
- Sequence of cro gene of bacteriophage lambdaNature, 1977
- X-Ray Structure of ProteinsPublished by Elsevier ,1977
- Autoregulation and Function of a Repressor in Bacteriophage LambdaScience, 1976
- Purification and properties of a DNA-binding protein with characteristics expected for the Cro protein of bacteriophage lambda, a repressor essential for lytic growth.Proceedings of the National Academy of Sciences, 1976
- CONTROL OF GENE EXPRESSION IN BACTERIOPHAGE LAMBDAAnnual Review of Genetics, 1973
- DEVELOPMENTAL PATHWAYS FOR THE TEMPERATE PHAGE: LYSIS VS LYSOGENYAnnual Review of Genetics, 1972