Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides.

@article{Mizutani2002ProteinsplicingRV,
  title={Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides.},
  author={Ryuta Mizutani and Satoru Nogami and Masato Kawasaki and Yoshikazu Ohya and Yasuhiro Anraku and Yoshinori Satow},
  journal={Journal of molecular biology},
  year={2002},
  volume={316 4},
  pages={919-29}
}
Protein splicing excises an internal intein segment from a protein precursor precisely, and concomitantly ligates flanking N and C-extein polypeptides at the respective sides of the precursor. Here, a series of precursor recombinants bearing 11 N-extein and ten C-extein residues is prepared for the intein of the Saccharomyces cerevisiae VMA1-derived homing endonuclease referred to as VDE and as PI-SceI. The recombinant with replacements of C284S, H362N, N737S, and C738S is chosen as a… CONTINUE READING

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