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

W. F. Anderson, D. H. Ohlendorf, Y. Takeda, B. W. Matthews

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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.

Original languageEnglish (US)
Pages (from-to)754-758
Number of pages5
Issue number5809
StatePublished - Dec 1 1981


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