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

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-fol...

Full description

Saved in:
Bibliographic Details
Published inNature (London) Vol. 290; no. 5809; p. 754
Main Authors Anderson, W F, Ohlendorf, D H, Takeda, Y, Matthews, B W
Format Journal Article
LanguageEnglish
Published England 30.04.1981
Subjects
Bacteriophage lambda
Carrier Proteins
DNA
DNA, Viral - metabolism
DNA-Binding Proteins
Macromolecular Substances
Nucleic Acid Conformation
Protein Binding
Protein Conformation
Repressor Proteins
Structure-Activity Relationship
Transcription Factors
Viral Proteins
X-Ray Diffraction
Online AccessGet more information

Cover

More Information
Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/290754a0