1F82

BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN

Summary for 1F82

• Entry DOI: 10.2210/pdb1f82/pdb
• Related: 1F83 3BTA
• Descriptor: BOTULINUM NEUROTOXIN TYPE B, ZINC ION (3 entities in total)
• Functional Keywords: zinc dependent protease, botulinum neurotoxin, toxin, hydrolase
• Biological source: Clostridium botulinum
• Cellular location: Botulinum neurotoxin B light chain: Secreted. Botulinum neurotoxin B heavy chain: Secreted: P10844
• Total number of polymer chains: 1
• Total formula weight: 49076.03

Authors

Hanson, M.A.,Stevens, R.C. (deposition date: 2000-06-28, release date: 2000-08-16, Last modification date: 2024-02-07)

Primary citation

Hanson, M.A.,Stevens, R.C.
Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution.
Nat.Struct.Biol., 7:687-692, 2000

PubMed Abstract: Botulinum neurotoxin serotype B is a zinc protease that disrupts neurotransmitter release by cleaving synaptobrevin-II (Sb2), one of three SNARE proteins involved in neuronal synaptic vesicle fusion. The three-dimensional crystal structure of the apo botulinum neurotoxin serotype B catalytic domain (BoNT/B-LC) has been determined to 2.2 A resolution, and the complex of cleaved Sb2 with the catalytic domain (Sb2-BoNT/B-LC) has been determined to 2.0 A resolution. A comparison of the holotoxin catalytic domain and the isolated BoNT/B-LC structure shows a rearrangement of three active site loops. This rearrangement exposes the BoNT/B active site. The Sb2-BoNT/B-LC structure illustrates two distinct binding regions, which explains the specificity of each botulinum neurotoxin for its synaptic vesicle protein. This observation provides an explanation for the proposed cooperativity between binding of full-length substrate and catalysis and suggest a mechanism of synaptobrevin proteolysis employed by the clostridial neurotoxins.

PubMed: 10932255
DOI: 10.1038/77997

Experimental method

X-RAY DIFFRACTION (2.2 Å)