Structural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15.

@article{Bhardwaj2008StructuralAF,
  title={Structural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15.},
  author={Kanchan Bhardwaj and Satheesh K. Palaninathan and Joanna Maria Ortiz Alcantara and Lillian Li Yi and Linda A. Guarino and James C. Sacchettini and Cheng Kao},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 6},
  pages={3655-64}
}
The severe acute respiratory syndrome (SARS) coronavirus encodes several RNA-processing enzymes that are unusual for RNA viruses, including Nsp15 (nonstructural protein 15), a hexameric endoribonuclease that preferentially cleaves 3' of uridines. We solved the structure of a catalytically inactive mutant version of Nsp15, which was crystallized as a hexamer. The structure contains unreported flexibility in the active site of each subunit. Substitutions in the active site residues serine 293 and… CONTINUE READING
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