The three-dimensional structure of trp repressor

  title={The three-dimensional structure of trp repressor},
  author={Richard Walter Schevitz and Z. Otwinowski and Andrzej J Joachimiak and Catherine L. Lawson and Paul B. Sigler},
The crystal structure of the Escherichia coli trp repressor has been solved to atomic resolution. The dimeric protein has a remarkable subunit interface in which five of each subunit's six helices are interlinked. The binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix–turn–helix motif and by moulding the details of the repressor's structure near the DNA binding surface. 
trp Repressor, A Crystallographic Study of Allostery in Genetic Regulation
The crystal structure of the E. coli trp repressor has been solved (1) and refined to 2.2 A. The two subunits (107 residues each) are related by an exact crystallographic dyad. Each subunit is
Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor
The three-dimensional crystal structure of met repressor shows a dimer of intertwined monomers, which do not have the helix-turn-helix motif characteristic of other bacterial repressor and activator structures, and is proposed to be a model for binding of several dimers to met operator regions.
Structure of the amino-terminal domain of phage 434 repressor at 2.0 A resolution.
The structure of trp RNA-binding attenuation protein
The crystal structure of the trp RNA-binding attenuation protein of Bacillus subtilis solved at 1.8 Å resolution reveals a novel structural arrangement in which the eleven subunits are stabilized
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
Crystal structure of trp represser/operator complex at atomic resolution
The crystal structure of the trp repressor/operator complex shows an extensive contact surface, including 24 direct and 6 solvent-mediated hydrogen bonds to the phosphate groups of the DNA. There are
Flexibility of the DNA‐binding domains of trp repressor
It is concluded that while L‐tryptophan binding is essential for forming a specific complex with trp operator DNA, the corepressor ligand does not lock the repressor into a single conformation that is complementary to the operator.
A Two-Dimensional NMR Study of the Complex of lac Repressor Headpiece with a 14 Base Pair lac Operator Fragment
Lac repressor of E. coli recognizes a 20 to 25 basepair DNA sequence called the lac operator, which blocks transcription of the genes coding for the lactose enzymes.


The operator-binding domain of λ repressor: structure and DNA recognition
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.
Three-dimensional structure of calmodulin
The three-dimensional structure of calmodulin has been determined crystallographically at 3.0 Å resolution and it is shown that each lobe binds two calcium ions through helix–loop–helix domains similar to those of other calcium-binding proteins.
Structure of the cro repressor from bacteriophage λ and its interaction with DNA
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.
The molecular basis of DNA–protein recognition inferred from the structure of cro repressor
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
Mutational studies with the trp repressor of Escherichia coli support the helix-turn-helix model of repressor recognition of operator DNA.
  • R. Kelley, C. Yanofsky
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1985
Observations with trpR nonsense mutants suggest that the first 67 residues of the repressor polypeptide are sufficient for subunit association.
The α-helix dipole and the properties of proteins
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
Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA
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.
Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda.
The second and third alpha-helices, alpha 2 and alpha 3, are shown to have essentially identical conformations in the two proteins, confirming the significance of the amino acid sequence homology previously noted between these and other DNA binding proteins in the region corresponding to these helices.
The N-terminal arms of λ repressor wrap around the operator DNA
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.