Structure of the cro repressor from bacteriophage λ and its interaction with DNA
Abstract
The three-dimensional structure of the 66-amino acid cro repressor protein of bacteriophage λ 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 α-helices of the represser, 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.
- Publication:
-
Nature
- Pub Date:
- April 1981
- DOI:
- 10.1038/290754a0
- Bibcode:
- 1981Natur.290..754A