The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules.

@article{Sugiura2000The2A,
  title={The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules.},
  author={Ikuko Sugiura and Osamu Nureki and Y Ugaji-Yoshikawa and Satoshi Kuwabara and Atsushi Shimada and Masaru Tateno and Bernard Lorber and Richard Gieg{\'e} and Dino Moras and Shigeyuki Yokoyama and Michiko Konno},
  journal={Structure},
  year={2000},
  volume={8 2},
  pages={197-208}
}
BACKGROUND The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. The 10 class I synthetases are considered to have in common the catalytic domain structure based on the Rossmann fold, which is totally different from the class II catalytic domain structure. The class I synthetases are further divided into three subclasses, a, b and c, according to sequence homology. No conserved structural features for tRNA recognition by class I synthetases have been established. RESULTS… CONTINUE READING
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