Structural basis of translational control by Escherichia coli threonyl tRNA synthetase

@article{TorresLarios2002StructuralBO,
  title={Structural basis of translational control by Escherichia coli threonyl tRNA synthetase},
  author={Alfredo Torres-Larios and Anne-Catherine Dock-Br{\'e}geon and Pascale Romby and Bernard Rees and Rajan Sankaranarayanan and Joël Caillet and M. Springer and Chantal Ehresmann and Bernard Ehresmann and Dino Moras},
  journal={Nature Structural Biology},
  year={2002},
  volume={9},
  pages={343-347}
}
Escherichia coli threonyl-tRNA synthetase (ThrRS) represses the translation of its own messenger RNA by binding to an operator located upstream of the initiation codon. The crystal structure of the complex between the core of ThrRS and the essential domain of the operator shows that the mRNA uses the recognition mode of the tRNA anticodon loop to initiate binding. The final positioning of the operator, upon which the control mechanism is based, relies on a characteristic RNA motif adapted to… 
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TLDR
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