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}
}
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. 
A phage repressor–operator complex at 7 Å resolution
TLDR
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
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
TLDR
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.
The three-dimensional structure of trp repressor
TLDR
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
TLDR
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
TLDR
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.
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TLDR
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
TLDR
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
TLDR
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
TLDR
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.
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TLDR
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TLDR
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TLDR
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