AB5 toxins.
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.
Merritt
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Department of Biological Structure, University of Washington, Seattle 98195, USA.
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D001427:Bacterial Toxins / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D019204:GTP-Binding Proteins / Q000378:metabolism; D005732:Gangliosides / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011956:Receptors, Cell Surface / Q000378:metabolism
D001427:Bacterial Toxins; D005732:Gangliosides; D006023:Glycoproteins; D011956:Receptors, Cell Surface; D019204:GTP-Binding Proteins