Peripheral insertion modulates the editing activity of the isolated CP1 domain of leucyl-tRNA synthetase.

@article{Liu2011PeripheralIM,
  title={Peripheral insertion modulates the editing activity of the isolated CP1 domain of leucyl-tRNA synthetase.},
  author={Ru-Juan Liu and Min Tan and Dao-hai Du and Bei-Si Xu and Gilbert Eriani and En-Duo Wang},
  journal={The Biochemical journal},
  year={2011},
  volume={440 2},
  pages={217-27}
}
A large insertion domain called CP1 (connective peptide 1) present in class Ia aminoacyl-tRNA synthetases is responsible for post-transfer editing. LeuRS (leucyl-tRNA synthetase) from Aquifex aeolicus and Giardia lamblia possess unique 20 and 59 amino acid insertions respectively within the CP1 that are crucial for editing activity. Crystal structures of AaLeuRS-CP1 [2.4 Å (1 Å=0.1 nm)], GlLeuRS-CP1 (2.6 Å) and the insertion deletion mutant AaLeuRS-CP1Δ20 (2.5 Å) were solved to understand the… CONTINUE READING

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