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

@article{Anderson1981StructureOT,
title={Structure of the cro repressor from bacteriophage $\lambda$ and its interaction with DNA},
author={Wayne F. Anderson and Douglas H. Ohlendorf and Yoshinori Takeda and Brian W. Matthews},
journal={Nature},
year={1981},
volume={290},
pages={754-758}
}
• Published 30 April 1981
• Biology, Chemistry
• Nature
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…
444 Citations
The molecular basis of DNA–protein recognition inferred from the structure of cro repressor
• Biology, Chemistry
Nature
• 1982
Recognition by cro repressor protein of its specific DNA binding sites appears to occur via multidentate hydrogen bonds between amino acid side chains of the protein and base-pair atoms in the major
The structure of plasmid‐encoded transcriptional repressor CopG unliganded and bound to its operator
• Biology
The EMBO journal
• 1998
The structure of the 45 amino acid transcriptional repressor, CopG, has been solved unliganded and bound to its target operator DNA, and it is revealed that the bihelical region of CopG has a role in oligomerization instead of DNA recognition.
How Cro and lambda-repressor distinguish between operators: the structural basis underlying a genetic switch.
• Biology
Proceedings of the National Academy of Sciences of the United States of America
• 1998
It appears that similar contacts to the invariant or almost invariant bps are used by both Cro and lambda-repressor to differentiate the operator sites as a group from other sites on the DNA.

## References

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Sequence of cro gene of bacteriophage lambda
• Biology
Nature
• 1977
The DNA sequence for the structural gene of a third represser, the Cro protein of lambda, is reported, of special interest both because of its small size and because genetic evidence suggests that it interacts with the same operator regions as does the cI protein, although the two proteins probably do not recognise exactly the same DNA bases.
Amino acid sequence of Cro regulatory protein of bacteriophage lambda
• Biology
Nature
• 1977
The amino acid sequence of Cro protein is reported, which appears to have an apparent role in regulation of DNA replication and is convenient for structural analysis because of its extremely small size.
Purification and properties of a DNA-binding protein with characteristics expected for the Cro protein of bacteriophage lambda, a repressor essential for lytic growth.
• Biology
Proceedings of the National Academy of Sciences of the United States of America
• 1976
The Cro protein specified by bacteriophage lambda is a repressor essential for normal lytic growth of the virus, thus having a physiological role distinct from that of cI, the repressor that
Mechanism of action of the cro protein of bacteriophage lambda.
• Biology
Proceedings of the National Academy of Sciences of the United States of America
• 1978
The mechanism of action of cro protein was probed by measuring its ability to protect DNA against methylation by dimethyl sulfate and its effect on transcription in vitro, and it was shown that two regulatory proteins can bind to the same three adjacent sites in DNA with markedly different consequences.
How lac Repressor Binds to DNA
• Biology
Nature
• 1972
A sequence of about fifty amino-acids at the N-terminus of the lac repressor is thought to bind directly to lac operator DNA. Although this length cannot make the conventional cleft, it could form a
Interactions between DNA-bound repressors govern regulation by the λ phage repressor
• Biology
• 1979
It is demonstrated that the effect of repressor in a lysogen on the activity of the promoter PRM can be changed from activation to repression by deletion of OR1, and mediated by protein-protein contacts between adjacent repressor dimers.