# The operator-binding domain of λ repressor: structure and DNA recognition

@article{Pabo1982TheOD,
title={The operator-binding domain of $\lambda$ repressor: structure and DNA recognition},
author={Carl O. Pabo and Mitchell Lewis},
journal={Nature},
year={1982},
volume={298},
pages={443-447}
}
• Published 29 July 1982
• Chemistry, Biology
• Nature
The structure of the operator-binding domain of the λ repressor has been determined at 3.2 Å resolution. This domain contains an extended N-terminal arm and five α-helices. Model-building studies of the repressor–operator complex suggest that α-helices, especially the N-terminal parts of these helices, may provide a useful surface for protein–DNA interactions.
402 Citations
A phage repressor–operator complex at 7 Å resolution
• Chemistry
Nature
• 1985
The crystal structure of a complex between the DNA-binding domain of phage 434 repressor and a synthetic 434 operator shows that the protein binds to B-form DNA with the second α-helix of a helix–turn–helix motif lying in the major groove.
Structure of the represser–operator complex of bacteriophage 434
• Chemistry, Biology
Nature
• 1987
The crystal structure of a specific complex between the DNA-binding domain of phage 434 represser and a synthetic 434 operator DNA shows interactions that determine sequence-dependent affinity. The
The N-terminal arms of λ repressor wrap around the operator DNA
• Biology, Chemistry
Nature
• 1982
It is suggested that the first few N-terminal residues of the λ repressor form an extended arm that reaches around the back of the DNA helix when repressor binds to the operator.
Structural basis of DNA-protein recognition.
• Biology, Chemistry
Trends in biochemical sciences
• 1989
The three-dimensional structure of trp repressor
• Chemistry, Biology
Nature
• 1985
The crystal structure of the Escherichia coli trp repressor has been solved to atomic resolution and the binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix–turn–helix motif.
Changing the binding specificity of a represser by redesigning an α-helix
• Biology, Chemistry
Nature
• 1985
It is shown that the binding specificity of the resulting hybrid protein, as measured in vivo and in vitro, was that of P22 repressor.
Homology among DNA-binding proteins suggests use of a conserved super-secondary structure
• Biology, Chemistry
Nature
• 1982
Model-building studies indicate that this structure is important in DNA binding, and it is suggested that it may be a common feature of many DNA-binding proteins.

## References

SHOWING 1-10 OF 19 REFERENCES
Structure of the cro repressor from bacteriophage λ and its interaction with DNA
• Biology, Chemistry
Nature
• 1981
The three-dimensional structure of the 66-amino acid cro repressor protein of bacteriophage λ suggests how it binds to its operator DNA and suggests a pair of 2-fold-related α-helices of the represser seem to be a major determinant in recognition and binding.
Regulatory functions of the λ repressor reside in the amino-terminal domain
• Biology
Nature
• 1979
The repressor of bacteriophage λ is a protein containing two domains of approximately equal size that bind specifically to λ operator DNA and mediate positive and negative control of λ transcription both in vitro and in vivo.
The N-terminal arms of λ repressor wrap around the operator DNA
• Biology, Chemistry
Nature
• 1982
It is suggested that the first few N-terminal residues of the λ repressor form an extended arm that reaches around the back of the DNA helix when repressor binds to the operator.
Homology among DNA-binding proteins suggests use of a conserved super-secondary structure
• Biology, Chemistry
Nature
• 1982
Model-building studies indicate that this structure is important in DNA binding, and it is suggested that it may be a common feature of many DNA-binding proteins.
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
Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA
• Biology, Chemistry
Nature
• 1981
The 2.9 Å resolution crystal structure of Escherichia coli catabolite gene activator protein (CAP) completed with cyclic AMP reveals two distinct structural domains separated by a cleft, suggesting that the CAP conversion of right- to left-handed DNA in a closed supercoil, is what activates transcription by RNA polymerase.
Primary structure of the lambda repressor.
• Biology, Chemistry
Biochemistry
• 1978
The complete covalent structure of the bacteriophage lambda repressor has been determined by sequential Edman degradation, gas chromatographic-mass spectrometric peptide sequencing, and DNA
α-Helix–double helix interaction shown in the structure of a protamine-transfer RNA complex and a nucleoprotamine model
• Biology, Chemistry
Nature
• 1978
A structural model for nucleoprotamine is proposed, suggesting that the protamine molecule changes its conformation from a random coil to a structure containing α helices on binding to tRNA, and that α-helical segment(s) of protamine bind approximately along a shallow groove of a double-helicals portion of tRNA.
The α-helix dipole and the properties of proteins
• Biology, Chemistry
Nature
• 1978
Phosphate moieties bind frequently at N-termini of helices in proteins. It is shown that this corresponds with an optimal interaction of the helix dipole and the charged phosphate. This favourable
The lambda repressor contains two domains.
• Biology
Proceedings of the National Academy of Sciences of the United States of America
• 1979
Calorimetry and other data show that lambda repressor consists of two domains joined by a "connector" 40 amino acids long that is sensitive to proteases and binds DNA, and the carboxyl-terminal domain oligomerizes.