Structure of the gangrene alpha-toxin: the beauty in the beast.
The crystal and molecular structure of the Clostridium perfringens alpha-toxin crowns over a century-long research into the mechanisms of pathogenesis of gas gangrene. The structure reveals a two-domain enzyme, with a catalytic all-helical N-terminal domain, and a C-terminal domain similar in its jelly-roll topology to those found in pancreatic lipase and lipoxygenases.
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D001427:Bacterial Toxins / Q000737:chemistry*; D001694:Biological Warfare; D002135:Calcium-Binding Proteins; D003016:Clostridium perfringens / Q000472:pathogenicity*; D018360:Crystallography, X-Ray; D005734:Gangrene / Q000209:etiology* / Q000473:pathology; D006801:Humans; D008049:Lipase / Q000737:chemistry; D008084:Lipoxygenase / Q000737:chemistry; D008958:Models, Molecular; D010179:Pancreas / Q000201:enzymology; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D010738:Type C Phospholipases / Q000737:chemistry*
D001427:Bacterial Toxins; D002135:Calcium-Binding Proteins; D008084:Lipoxygenase; D008049:Lipase; D010738:Type C Phospholipases; C040649:alpha toxin, Clostridium perfringens