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Literature summary for 3.4.24.69 extracted from

  • Jin, R.; Rummel, A.; Binz, T.; Brunger, A.T.
    Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity (2006), Nature, 444, 1092-1095.
    View publication on PubMed

Application

Application Comment Organism
drug development botulinum toxins are targets for rational development of preventive vaccines or inhibitors Clostridium botulinum
additional information botulinum neurotoxins are biological hazards to humans and a serious potential bioweapon threat Clostridium botulinum

Cloned(Commentary)

Cloned (Comment) Organism
expression of Strep-tagged HCB-Syt-II fusion protein Clostridium botulinum

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant protein consisting of the receptor-binding domain of botulinum neurotoxin serotype B fused to the luminal domain of synaptotagmin II, vapour diffusion method, 20°C, using first 13% PEG 6000 and 0.1 M HEPES pH 7.0, and second, 0.8 M sodium citrate, pH 6.5, X-ray diffraction structure detremination and analysis at 2.15 A resolution, molecular replacement and modeling Clostridium botulinum

Protein Variants

Protein Variants Comment Organism
additional information construction of a HCB-Syt-II fusion protein by fusion of the HC fragment of BoNT/B, residues 858-1291, with the luminal domain of rat Syt-II, residues 8–61, connected by a 15-residue linker, PPTPGSAWSHPQFEK, including a Strep-tag, site-directed mutagenesis analysis of the toxin-receptor binding site in BoNT/B and in the luminal domains of Syt-I and Syt-II, overview Clostridium botulinum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Clostridium botulinum BoNTs bind with high specificity at neuromuscular junctions and they impair exocytosis of synaptic vesicles containing acetylcholine through specific proteolysis of SNAREs, soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors, which constitute part of the synaptic vesicle fusion machinery, botulinum neurotoxins cause the neuroparalytic syndrome of botulism, BoNTs are biological hazard to humans and a serious potential bioweapon threat with a lethal dose of 1 ng/kg body weight ?
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Organism

Organism UniProt Comment Textmining
Clostridium botulinum
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information BoNTs bind with high specificity at neuromuscular junctions and they impair exocytosis of synaptic vesicles containing acetylcholine through specific proteolysis of SNAREs, soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors, which constitute part of the synaptic vesicle fusion machinery, botulinum neurotoxins cause the neuroparalytic syndrome of botulism, BoNTs are biological hazard to humans and a serious potential bioweapon threat with a lethal dose of 1 ng/kg body weight Clostridium botulinum ?
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additional information the the receptor-binding domain of botulinum neurotoxin serotype B binds to the luminal domain of synaptotagmin II, i.e. Syt-II, interaction occurs at both neutral and acidic endosomal pH, residues Glu44 to Lys60 become structured with residues Phe47 to Ile58 forming an alpha-helix, the HCB-Syt-II complex is stabilized by extensive intermolecular interactions involving two pronounced pockets on the HCB surface, structure, overview, high selectivity of BoNT/B among synaptotagmin I and II isoforms Clostridium botulinum ?
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Synonyms

Synonyms Comment Organism
BoNT/B
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Clostridium botulinum
botulinum neurotoxin B
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Clostridium botulinum
botulinum neurotoxin serotype B
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Clostridium botulinum
HCB
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Clostridium botulinum