2XSC

Crystal structure of the cell-binding B oligomer of verotoxin-1 from E. coli

Replaces:  1BOV

Summary for 2XSC

• Entry DOI: 10.2210/pdb2xsc/pdb
• Related: 1OJF
• Descriptor: SHIGA-LIKE TOXIN 1 SUBUNIT B, ZINC ION (3 entities in total)
• Functional Keywords: toxin
• Biological source: ESCHERICHIA COLI
• Cellular location: Secreted: P69178
• Total number of polymer chains: 5
• Total formula weight: 38689.40

Authors

Stein, P.E.,Boodhoo, A.,Tyrrell, G.J.,Brunton, J.L.,Oeffner, R.D.,Bunkoczi, G.,Read, R.J. (deposition date: 2010-09-27, release date: 2010-10-13, Last modification date: 2024-11-13)

Primary citation

Stein, P.E.,Boodhoo, A.,Tyrrell, G.J.,Brunton, J.L.,Read, R.J.
Crystal Structure of the Cell-Binding B Oligomer of Verotoxin-1 from E. Coli.
Nature, 355:748-, 1992

PubMed Abstract: The Shiga toxin family, a group of cytotoxins associated with diarrhoeal diseases and the haemolytic uraemic syndrome, includes Shiga toxin from Shigella dysenteriae type 1 and verotoxins produced by enteropathogenic Escherichia coli. The family belongs to the A-B class of bacterial toxins, which includes the cholera toxin family, pertussis and diphtheria toxins. These toxins all have bipartite structures consisting of an enzymatic A subunit associated with a B oligomer which binds to specific cell-surface receptors, but their amino-acid sequences and pathogenic mechanisms differ. We have determined the crystal structure of the B oligomer of verotoxin-1 from E. coli. The structure unexpectedly resembles that of the B oligomer of the cholera toxin-like heat-labile enterotoxin from E. coli, despite the absence of detectable sequence similarity between these two proteins. This result implies a distant evolutionary relationship between the Shiga toxin and cholera toxin families. We suggest that the cell surface receptor-binding site lies in a cleft between adjacent subunits of the B pentamer, providing a potential target for drugs and vaccines to prevent toxin binding and effect.

PubMed: 1741063
DOI: 10.1038/355748A0

Experimental method

X-RAY DIFFRACTION (2.052 Å)