@text
Botulinum neurotoxin serotype A, the molecule responsible for botulism, is a 150 kDa protein comprised of three 50 kDa functional domains.  The protein consists of two chains, 50 kDa and 100 kDa, which are linked by a disulfide bond.   Amino acids 1 - 437 make up the catlytic domain, 448 - 872 make up the translocation domain, and 873-1295 make up the receptor binding domain.

Toxicity of botulinum toxin invloves receptor binding (to cholinergic neurons) and endocytosis of the holotoxin.  Once inside the endosome, pore formation is induced, the toxin is cleaved between the translocation domain and the catalytic domain, and the catalytic domain is translocated to the cytosol.

The catalytic domain is a zinc - dependent metalloproteinase which interferes with synaptic vesicle fusion by cleaving one of three proteins involved in this process.  The specificity of the target protein depends on the serotype of the toxin, as does the specificity of the receptor protein.

Reference: Lacy, D.B., Tepp, W., Cohen, A.C., DasGupta, B.R. and Stevens, R.C. (1998). Crystal structure of botulinum neurotoxin type A and implications for toxicity.  Nature Structural Biology, vol. 5, no. 10; 898-902.














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The whole molecule is shown here as a ribbon diagram, and each of the next three views focuses on one of the independent functional domains of the protein.
View 2 shows the binding domain.
View 3 shows the translocation domain.
View 4 shows the catalytic domain.

coordinates from file: 3BTA (Botulinum).pdb 
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