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Nature. 1981 Apr 30;290(5809):754-8.

Structure of the cro repressor from bacteriophage lambda and its interaction with DNA.

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.

PMID:
6452580
DOI:
10.1038/290754a0
[Indexed for MEDLINE]

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