AB5 toxins

Curr Opin Struct Biol. 1995 Apr;5(2):165-71. doi: 10.1016/0959-440x(95)80071-9.


Crystal structures of shiga and pertussis toxins have recently revealed a remarkable degree of structural homology among the members of the AB5 class of bacterial toxins. Other structures have provided a detailed view of the molecular basis of receptor binding specificity of cholera toxin, and of the heat-labile enterotoxin of Escherichia coli. These structures also provide tantalizing, but as yet incomplete, information on the site of ADP-ribosylation in the homologous A-subunits of the Escherichia coli heat-labile toxin, cholera toxin, and pertussis toxin.

Publication types

  • Review

MeSH terms

  • Bacterial Toxins / chemistry*
  • Bacterial Toxins / classification
  • Bacterial Toxins / metabolism
  • Binding Sites
  • Crystallography, X-Ray
  • GTP-Binding Proteins / metabolism
  • Gangliosides / metabolism
  • Glycoproteins / chemistry
  • Glycoproteins / metabolism
  • Models, Molecular
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Tertiary
  • Receptors, Cell Surface / metabolism


  • Bacterial Toxins
  • Gangliosides
  • Glycoproteins
  • Receptors, Cell Surface
  • GTP-Binding Proteins