Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation.

@article{Kavran2007StructureOP,
  title={Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation.},
  author={Jennifer M Kavran and Sarath B. Gundllapalli and Patrick O'Donoghue and Markus Englert and Dieter S{\"o}ll and Thomas A Steitz},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 27},
  pages={11268-73}
}
Pyrrolysine (Pyl), the 22nd natural amino acid and genetically encoded by UAG, becomes attached to its cognate tRNA by pyrrolysyl-tRNA synthetase (PylRS). We have determined three crystal structures of the Methanosarcina mazei PylRS complexed with either AMP-PNP, Pyl-AMP plus pyrophosphate, or the Pyl analogue N-epsilon-[(cylopentyloxy)carbonyl]-L-lysine plus ATP. The structures reveal that PylRS utilizes a deep hydrophobic pocket for recognition of the Pyl side chain. A comparison of these… CONTINUE READING