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Crystal structure of the holotoxino from Shigella dysenteriae at 2.5 Å resolution

Nature Structural Biology volume 1, pages 59–64 (1994)Cite this article

Abstract

Shigella dysenteriae is the pathogen responsible for the severe form of dysentery in humans. It produces Shiga toxin, the prototype of a family of closely related bacterial protein toxins. We have determined the structure of the holotoxin, an AB5 hexamer, by X–ray crystallography. The five B subunits form a pentameric ring, encircling a helix at the carboxy terminus of the A subunit. The A subunit interacts with the B pentamer via this C–terminal helix and a four–stranded mixed β–sheet. The fold of the rest of the A subunit is similar to that of the A chain of the plant toxin ricin; both are N–glycosidases. However, the active site in the bacterial holotoxin is blocked by a segment of polypeptide chain. These residues of the A subunit would be released as part of the activation mechanism of the toxin.

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Authors and Affiliations

  1. Medical Research Council of Canada Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada

    Marie E. Fraser, Maia M. Chernaia & Michael N.G. James

  2. T6G 2H7, Moscow, Russia

    Marie E. Fraser, Maia M. Chernaia & Michael N.G. James

  3. Englehardt Institute of Molecular Biology, Academy of Sciences of Russia, University of Oslo Center for Medical Studies, Vavilov str 32, Moscow, Russia

    Yuri V. Kozlov

Authors
  1. Marie E. Fraser
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  2. Maia M. Chernaia
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  3. Yuri V. Kozlov
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  4. Michael N.G. James
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Fraser, M., Chernaia, M., Kozlov, Y. et al. Crystal structure of the holotoxino from Shigella dysenteriae at 2.5 Å resolution. Nat Struct Mol Biol 1, 59–64 (1994). https://doi.org/10.1038/nsb0194-59

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