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-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.
D010582:Bacteriophage lambda; D002352:Carrier Proteins; D004247:DNA; D004279:DNA, Viral / Q000378:metabolism*; D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011487:Protein Conformation; D012097:Repressor Proteins; D013329:Structure-Activity Relationship; D014157:Transcription Factors; D014764:Viral Proteins; D014961:X-Ray Diffraction
D002352:Carrier Proteins; D004279:DNA, Viral; D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D012097:Repressor Proteins; D014157:Transcription Factors; D014764:Viral Proteins; D004247:DNA