Crystal Structure of PI-SceI, a Homing Endonuclease with Protein Splicing Activity

@article{Duan1997CrystalSO,
  title={Crystal Structure of PI-SceI, a Homing Endonuclease with Protein Splicing Activity},
  author={X. Duan and Frederick S. Gimble and Florante A. Quiocho},
  journal={Cell},
  year={1997},
  volume={89},
  pages={555-564}
}
PI-Scel is a bifunctional yeast protein that propagates its mobile gene by catalyzing protein splicing and site-specific DNA double-strand cleavage. Here, we report the 2.4 A crystal structure of the PI-Scel protein. The structure is composed of two separate domains (I and II) with novel folds and different functions. Domain I, which is elongated and formed largely from seven beta sheets, harbors the N and C termini residues and two His residues that are implicated in protein splicing. Domain… 
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Structural stability and endonuclease activity of a PI-SceI GFP-fusion protein
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