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

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

doi:10.1038/290754a0

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

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

^*Corresponding author for this work

Biochemistry and Molecular Genetics

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418 Scopus citations

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.

Original language	English (US)
Pages (from-to)	754-758
Number of pages	5
Journal	Nature
Volume	290
Issue number	5809
DOIs	https://doi.org/10.1038/290754a0
State	Published - 1981

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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.",

author = "Anderson, {W. F.} and Ohlendorf, {D. H.} and Y. Takeda and Matthews, {B. W.}",

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AU - Anderson, W. F.

AU - Ohlendorf, D. H.

AU - Takeda, Y.

AU - Matthews, B. W.

PY - 1981

Y1 - 1981

N2 - 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.

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

Abstract

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