• Biology, Medicine
  • Published in Nature Structural Biology 2002
  • DOI:10.1038/nsb853

Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI

@article{Roey2002CatalyticDS,
  title={Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI},
  author={Patrick Van Roey and Lisa Meehan and Joseph C. Kowalski and Marlene Belfort and Victoria Derbyshire},
  journal={Nature Structural Biology},
  year={2002},
  volume={9},
  pages={806-811}
}
I-TevI, a member of the GIY-YIG family of homing endonucleases, consists of an N-terminal catalytic domain and a C-terminal DNA-binding domain joined by a flexible linker. The GIY-YIG motif is in the N-terminal domain of I-TevI, which corresponds to a phylogenetically widespread catalytic cartridge that is often associated with mobile genetic elements. The crystal structure of the catalytic domain of I-TevI, the first of any GIY-YIG endonuclease, reveals a novel α/β-fold with a central three… CONTINUE READING

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