1f82
From Proteopedia
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BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN
Overview
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.
About this Structure
1F82 is a Single protein structure of sequence from Clostridium botulinum with ZN as ligand. Active as Bontoxilysin, with EC number 3.4.24.69 Full crystallographic information is available from OCA.
Reference
Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution., Hanson MA, Stevens RC, Nat Struct Biol. 2000 Aug;7(8):687-92. PMID:10932255
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