1CA1

ALPHA-TOXIN FROM CLOSTRIDIUM PERFRINGENS

Summary for 1CA1

• Entry DOI: 10.2210/pdb1ca1/pdb
• Descriptor: ALPHA-TOXIN, ZINC ION, CADMIUM ION, ... (4 entities in total)
• Functional Keywords: zinc phospholipase c, gangrene determinant, c2 domain, ca and membrane binding, hydrolase
• Biological source: Clostridium perfringens
• Total number of polymer chains: 1
• Total formula weight: 44030.20

Authors

Naylor, C.E.,Basak, A.K.,Titball, R.W. (deposition date: 1998-04-22, release date: 1999-05-04, Last modification date: 2024-04-03)

Primary citation

Naylor, C.E.,Eaton, J.T.,Howells, A.,Justin, N.,Moss, D.S.,Titball, R.W.,Basak, A.K.
Structure of the key toxin in gas gangrene.
Nat.Struct.Biol., 5:738-746, 1998

PubMed Abstract: Clostridium perfringens alpha-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 phospholipase C (PC-PLC). The C-terminal domain shows a strong structural analogy to eukaryotic calcium-binding C2 domains. We believe this is the first example of such a domain in prokaryotes. This type of domain has been found to act as a phospholipid and/or calcium-binding domain in intracellular second messenger proteins and, interestingly, these pathways are perturbed in cells treated with alpha-toxin. Finally, a possible mechanism for alpha-toxin attack on membrane-packed phospholipid is described, which rationalizes its toxicity when compared to other, non-haemolytic, but homologous phospholipases C.

PubMed: 9699639
DOI: 10.1038/1447

Experimental method

X-RAY DIFFRACTION (1.9 Å)