L-arginine recognition by yeast arginyl-tRNA synthetase.

@article{Cavarelli1998LarginineRB,
  title={L-arginine recognition by yeast arginyl-tRNA synthetase.},
  author={Jean Cavarelli and B{\'e}n{\'e}dicte Delagoutte and Gilbert Eriani and Jean Gangloff and Dino Moras},
  journal={The EMBO journal},
  year={1998},
  volume={17 18},
  pages={5438-48}
}
The crystal structure of arginyl-tRNA synthetase (ArgRS) from Saccharomyces cerevisiae, a class I aminoacyl-tRNA synthetase (aaRS), with L-arginine bound to the active site has been solved at 2.75 A resolution and refined to a crystallographic R-factor of 19.7%. ArgRS is composed predominantly of alpha-helices and can be divided into five domains, including the class I-specific active site. The N-terminal domain shows striking similarity to some completely unrelated proteins and defines a… CONTINUE READING

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