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spinqualitylabelsall models 1bov, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE CELL-BINDING B OLIGOMER OF VEROTOXIN-1 FROM E. COLI

Overview

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.

About this Structure

1BOV is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the cell-binding B oligomer of verotoxin-1 from E. coli., Stein PE, Boodhoo A, Tyrrell GJ, Brunton JL, Read RJ, Nature. 1992 Feb 20;355(6362):748-50. PMID:1741063

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