Structure of the gangrene alpha-toxin: the beauty in the beast.

Abstract	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.
Authors	Z S Derewenda, T W Martin
Journal	Nature structural biology (Nat Struct Biol) Vol. 5 Issue 8 Pg. 659-62 (Aug 1998) ISSN: 1072-8368 [Print] United States
PMID	9699620 (Publication Type: Comment, Comparative Study, News)
Chemical References	Bacterial Toxins Calcium-Binding Proteins Lipoxygenase Lipase Type C Phospholipases alpha toxin, Clostridium perfringens
Topics	Bacterial Toxins (chemistry) Biological Warfare Calcium-Binding Proteins Clostridium perfringens (pathogenicity) Crystallography, X-Ray Gangrene (etiology, pathology) Humans Lipase (chemistry) Lipoxygenase (chemistry) Models, Molecular Pancreas (enzymology) Protein Conformation Protein Structure, Secondary Type C Phospholipases (chemistry)

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