The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I

@article{Foster2000TheSB,
  title={The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I},
  author={Paul G. Foster and Lixuan L. Huang and Daniel V Santi and Robert Michael Stroud},
  journal={Nature Structural Biology},
  year={2000},
  volume={7},
  pages={23-27}
}
Pseudouridine synthases catalyze the isomerization of specific uridines to pseudouridine in a variety of RNAs, yet the basis for recognition of the RNA sites or how they catalyze this reaction is unknown. The crystal structure of pseudouridine synthase I from Escherichia coli, which, for example, modifies positions 38, 39 and/or 40 in tRNA, reveals a dimeric protein that contains two positively charged, RNA-binding clefts along the surface of the protein. Each cleft contains a highly conserved… CONTINUE READING

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Modification and editing of RNA

  • H. Grosjean, R. Benne
  • 1998

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