The structure of I-Crel, a Group I intron-encoded homing endonuclease

@article{Heath1997TheSO,
  title={The structure of I-Crel, a Group I intron-encoded homing endonuclease},
  author={Patrick J. Heath and Kathryn M. Stephens and Raymond J. Monnat and Barry L. Stoddard},
  journal={Nature Structural Biology},
  year={1997},
  volume={4},
  pages={468-476}
}
The structure of I-Crel provides the first view of a protein encoded by a gene within an intron. This endonuclease recognizes a long DNA site ∼20 base pairs in length and facilitates the lateral transfer of that intron. The protein exhibits a DNA-binding surface consisting of four antiparallel β-strands that form a 20 Å wide groove which is over 70 Å long. The architecture of this fold is different from that of the TATA binding protein, TBP, which also contains an antiparallel β-saddle. The… CONTINUE READING

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