Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli

Nature. 1991 May 30;351(6325):371-7. doi: 10.1038/351371a0.

Abstract

Examination of the structure of Escherichia coli heat-labile enterotoxin in the AB5 complex at a resolution of 2.3A reveals that the doughnut-shaped B pentamer binds the enzymatic A subunit using a hairpin of the A2 fragment, through a highly charged central pore. Putative ganglioside GM1-binding sites on the B subunits are more than 20A removed from the membrane-crossing A1 subunit. This ADP-ribosylating (A1) fragment of the toxin has structural homology with the catalytic region of exotoxin A and hence also to diphtheria toxin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Toxins* / chemistry
  • Bacterial Toxins* / metabolism
  • Binding Sites
  • Computer Graphics
  • Crystallography
  • Enterotoxins* / chemistry
  • Enterotoxins* / metabolism
  • Escherichia coli
  • Escherichia coli Proteins*
  • Gangliosides / metabolism
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • NAD / metabolism
  • Protein Conformation
  • X-Ray Diffraction

Substances

  • Bacterial Toxins
  • Enterotoxins
  • Escherichia coli Proteins
  • Gangliosides
  • Macromolecular Substances
  • NAD
  • heat-labile enterotoxin, E coli