Enzyme structure with two catalytic sites for double-sieve selection of substrate.

@article{Nureki1998EnzymeSW,
  title={Enzyme structure with two catalytic sites for double-sieve selection of substrate.},
  author={Osamu Nureki and Dmitry G. Vassylyev and Masaru Tateno and Atsushi Shimada and Takashi Nakama and Shuya Fukai and Michiko Konno and Tamara L. Hendrickson and Paul R. Schimmel and Shigeyuki Yokoyama},
  journal={Science},
  year={1998},
  volume={280 5363},
  pages={578-82}
}
High-fidelity transfers of genetic information in the central dogma can be achieved by a reaction called editing. The crystal structure of an enzyme with editing activity in translation is presented here at 2.5 angstroms resolution. The enzyme, isoleucyl-transfer RNA synthetase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing" step, the synthetase itself rapidly hydrolyzes only the… CONTINUE READING

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