Crystal structure of trp represser/operator complex at atomic resolution

@article{Otwinowski1988CrystalSO,
  title={Crystal structure of trp represser/operator complex at atomic resolution},
  author={Z. Otwinowski and Richard Walter Schevitz and R.-g. Zhang and Catherine L. Lawson and Andrzej J Joachimiak and Ronen Marmorstein and Ben F. Luisi and Paul B. Sigler},
  journal={Nature},
  year={1988},
  volume={335},
  pages={321-329}
}
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 no direct hydrogen bonds or non-polar contacts to the bases that can explain the repressor's specificity for the operator sequence. Rather, the sequence seems to be recognized indirectly through its effects on the geometry of the phosphate backbone, which in turn permits the formation of a stable… 
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TLDR
The decrease of the number of hydrogen bonds between protein and DNA backbone could be the initial step of the dissociation process of the trp‐repressor operator complex, or in other words an intermediate complex conformation of the association process.
Conserved residues make similar contacts in two repressor-operator complexes.
TLDR
Structural comparisons appear to rule out any simple "recognition code" at the level of detailed side chain-base pair interactions in the helix-turn-helix (HTH) region.
Probing the Interface of the trp Repressor–Operator Complex Using Operator Sequences Containing Isosteric Base-Pair Analogues☆
TLDR
A series of base pair analogues, dI-dM and dD-dU, have been used in place of the native dA-dT and dG-dC residues to probe the interface between the trp repressor and its operator sequence, resulting in differences in binding by these analogue sequences.
Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor
TLDR
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.
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