Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase.

@article{Crepin2003UseOA,
  title={Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase.},
  author={Thibaut Crepin and Emmanuelle Schmitt and Yves Mechulam and Peter B Sampson and Mark D Vaughan and J F Honek and Sylvain Blanquet},
  journal={Journal of molecular biology},
  year={2003},
  volume={332 1},
  pages={59-72}
}
Binding of methionine to methionyl-tRNA synthetase (MetRS) is known to promote conformational changes within the active site. However, the contribution of these rearrangements to enzyme catalysis is not fully understood. In this study, several methionine and methionyl adenylate analogues were diffused into crystals of the monomeric form of Escherichia coli methionyl-tRNA synthetase. The structures of the corresponding complexes were solved at resolutions below 1.9A and compared to those of the… CONTINUE READING

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