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

Nature volume 290, pages 754–758 (1981)Cite this article

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.

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Authors and Affiliations

  1. Institute of Molecular Biology and Department of Physics, University of Oregon, Eugene, Oregon, 97403, USA

    W. F. Anderson, D. H. Ohlendorf & B. W. Matthews

  2. MRC Group on Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada, T6G 2H7

    W. F. Anderson

  3. Chemistry Department, University of Maryland, Baltimore County, Catonsville, Maryland, 21228, USA

    Y. Takeda

Authors
  1. W. F. Anderson
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  2. D. H. Ohlendorf
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  3. Y. Takeda
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  4. B. W. Matthews
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Anderson, W., Ohlendorf, D., Takeda, Y. et al. Structure of the cro repressor from bacteriophage λ and its interaction with DNA. Nature 290, 754–758 (1981). https://doi.org/10.1038/290754a0

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