Crystal structure of the met represser–operator complex at 2.8 Å resolution reveals DNA recognition by β-strands

@article{Somers1992CrystalSO,
  title={Crystal structure of the met represser–operator complex at 2.8 Å resolution reveals DNA recognition by $\beta$-strands},
  author={William Stuart Somers and Simon E V Phillips},
  journal={Nature},
  year={1992},
  volume={359},
  pages={387-393}
}
The crystal structure of the met represser–operator complex shows two dimeric repressor molecules bound to adjacent sites 8 base pairs apart on an 18-base-pair DNA fragment. Sequence specificity is achieved by insertion of double-stranded antiparallel protein β-ribbons into the major groove of B-form DNA, with direct hydrogen-bonding between amino-acid side chains and the base pairs. The repressor also recognizes sequence-dependent distortion or flexibility of the operator phosphate backbone… 
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TLDR
It is demonstrated that recognition of operator sequences occurs through side chains in the β-strand motif and that dimer–dimer interactions are required for effective repression.
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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
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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