ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding.

@article{Sekine2003ATPBB,
  title={ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding.},
  author={S. Sekine and Osamu Nureki and Daniel Y Dubois and St{\'e}phane Bernier and Robert Ch{\^e}nevert and Jacques Lapointe and Dmitry G. Vassylyev and Shigeyuki Yokoyama},
  journal={The EMBO journal},
  year={2003},
  volume={22 3},
  pages={
          676-88
        }
}
Aminoacyl-tRNA synthetases catalyze the formation of an aminoacyl-AMP from an amino acid and ATP, prior to the aminoacyl transfer to tRNA. A subset of aminoacyl-tRNA synthetases, including glutamyl-tRNA synthetase (GluRS), have a regulation mechanism to avoid aminoacyl-AMP formation in the absence of tRNA. In this study, we determined the crystal structure of the 'non-productive' complex of Thermus thermophilus GluRS, ATP and L-glutamate, together with those of the GluRS.ATP, GluRS.tRNA.ATP and… CONTINUE READING
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