Structure of the key toxin in gas gangrene

@article{Naylor1998StructureOT,
  title={Structure of the key toxin in gas gangrene},
  author={Claire E. Naylor and Julian T. Eaton and Angela M Howells and Neil Justin and David S. Moss and Richard W Titball and Ajit K. Basak},
  journal={Nature Structural \&Molecular Biology},
  year={1998},
  volume={5},
  pages={738-746}
}
Clostridium perfringens α-toxin is the key virulence determinant in gas gangrene and has also been implicated in the pathogenesis of sudden death syndrome in young animals. The toxin is a 370-residue, zinc metalloenzyme that has phospholipase C activity, and can bind to membranes in the presence of calcium. The crystal structure of the enzyme reveals a two-domain protein. The N-terminal domain shows an anticipated structural similarity to Bacillus cereus phosphatidylcholine-specific… 

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The data support the proposed role of the 70-90 loop in the recognition of membrane phospholipids and provide key evidence in support of the hypothesis that the hydrolysis of both phosphatidylcholine and sphingomyelin are required for the cytolytic and toxic activity ofospholipases.
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