Structure and catalytic mechanism of eukaryotic selenocysteine synthase.

@article{Ganichkin2008StructureAC,
  title={Structure and catalytic mechanism of eukaryotic selenocysteine synthase.},
  author={Oleg M. Ganichkin and Xueming Xu and Bradley A. Carlson and Heiko Mix and Dolph Lee Hatfield and Vadim N. Gladyshev and Markus C Wahl},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 9},
  pages={5849-65}
}
In eukaryotes and Archaea, selenocysteine synthase (SecS) converts O-phospho-L-seryl-tRNA [Ser]Sec into selenocysteyl-tRNA [Ser]Sec using selenophosphate as the selenium donor compound. The molecular mechanisms underlying SecS activity are presently unknown. We have delineated a 450-residue core of mouse SecS, which retained full selenocysteyl-tRNA [Ser]Sec synthesis activity, and determined its crystal structure at 1.65 A resolution. SecS exhibits three domains that place it in the fold type I… CONTINUE READING

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