Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA

@article{Mckay1981StructureOC,
  title={Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA},
  author={David B. Mckay and Thomas A. Steitz},
  journal={Nature},
  year={1981},
  volume={290},
  pages={744-749}
}
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. The smaller carboxy-terminal domain is presumed to bind DNA while the amino-terminal domain is seen to bind cyclic AMP. Model building studies suggest that CAP binds to left-handed B-type DNA, contacting its major groove via two a-helices. It is possible that the CAP conversion of right- to left-handed DNA in a… 
The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer.
  • J. Passner, T. Steitz
  • Chemistry, Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1997
The 2.2 A resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with cAMP and a 46-bp DNA fragment reveals a second cAMP molecule bound to each
Catabolite activator protein: DNA binding and transcription activation.
Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees
The 3 angstrom resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with a 30-base pair DNA sequence shows that the DNA is bent by 90 degrees. This
Structure of the lambda complex at 2.5 A resolution: details of the repressor-operator interactions
The crystal structure of a complex containing the DNA-binding domain of lambda repressor and a lambda operator site was determined at 2.5 A resolution and refined to a crystallographic R factor of
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References

SHOWING 1-10 OF 45 REFERENCES
Structure of the cro repressor from bacteriophage λ and its interaction with DNA
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.
Interaction of the cAMP receptor protein with the lac promoter.
TLDR
The contacts inferred from this photochemical probe and the results of nucleolytic attack of this complex by exonuclease III support a model where the cyclic AMP receptor protein binds to the promoter making symmetrical contacts with one face of the double helix and then stimulates transcription through contacts with RNA polymerase.
Isolation of amino-terminal fragment of lactose repressor necessary for DNA binding.
TLDR
The monomeric headpieces show the relatively weak binding to nonoperator DNA but not the highly specific and strong binding to operator DNA typical for tetrameric lac repressor.
Amino-terminal fragments of Escherichia coli lac repressor bind to DNA
TLDR
The N-terminal fragments obtained by selective tryptic cleavage of native lac repressor retain the ability to bind DNA and form complexes which resemble those of tetrameric repressor with non-operator DNA.
Purification and DNA-binding properties of the catabolite gene activator protein.
  • A. Riggs, G. Reiness, G. Zubay
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1971
TLDR
CGA protein seems to be a new type of regulatory protein: a DNA-binding activator that activates the lac operon by binding to the DNA under the influence of cAMP.
How lac Repressor Binds to DNA
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
Interaction site of Escherichia coli cyclic AMP receptor protein on DNA of galactose operon promoters.
TLDR
The results indicate that cAMP-CRP binds to gal DNA in a segment located between 50 and 24 base pairs preceding the P1 start point for transcription, which suggests that protein-protein interactions between RNA polymerase and cAMP play an important role in transcription initiation at the gal and possibly other camp-dependent promoters.
The lambda repressor contains two domains.
TLDR
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.
RNA polymerase unwinds an 11-base pair segment of a phage T7 promoter
TLDR
A new technique described here directly proves unwinding and furthermore identifies the exact region thatRNA polymerase opens in the A3 promoter of phage T7, one of three strong E. coli RNA polymerase promoters used early in the life cycle of phages T7.
...
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5
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