Binding of adenine to Stx2, the protein toxin from Escherichia coli O157:H7.

@article{Fraser2006BindingOA,
  title={Binding of adenine to Stx2, the protein toxin from Escherichia coli O157:H7.},
  author={Marie E. Fraser and Maia M. Cherney and Paola Marcato and George L. Mulvey and Glen D. Armstrong and Michael N. G. James},
  journal={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2006},
  volume={62 Pt 7},
  pages={
          627-30
        }
}
Stx2 is a protein toxin whose catalytic subunit acts as an N-glycosidase to depurinate a specific adenine base from 28S rRNA. In the holotoxin, the catalytic portion, A1, is linked to the rest of the A subunit, A2, and A2 interacts with the pentameric ring formed by the five B subunits. In order to test whether the holotoxin is active as an N-glycosidase, Stx2 was crystallized in the presence of adenosine and adenine. The crystals diffracted to approximately 1.8 angstroms and showed clear… CONTINUE READING

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