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

Nature Structural Biology volume 1, pages 5964 (1994) | Download Citation

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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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Affiliations

  1. Medical Research Council of Canada Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2H7, Moscow, Russia

    • Marie E. Fraser
    • , Maia M. Chernaia
    •  & Michael N.G. James
  2. Englehardt Institute of Molecular Biology, Academy of Sciences of Russia, Vavilov str 32; University of Oslo Center for Medical Studies, Moscow, Russia

    • Yuri V. Kozlov

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https://doi.org/10.1038/nsb0194-59

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