1F31

CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH A TRISACCHARIDE

Summary for 1F31

• Entry DOI: 10.2210/pdb1f31/pdb
• Related: 1EPW
• Descriptor: BOTULINUM NEUROTOXIN TYPE B, N-acetyl-alpha-neuraminic acid-(2-3)-alpha-D-galactopyranose-(1-4)-alpha-D-glucopyranose, ZINC ION, ... (5 entities in total)
• Functional Keywords: botulinum, zinc, metalloprotease, transmembrane, neurotoxin, complex, ganglioside, toxin
• 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: 151628.40

Authors

Swaminathan, S.,Eswaramoorthy, S. (deposition date: 2000-05-31, release date: 2000-11-01, Last modification date: 2024-11-06)

Primary citation

Swaminathan, S.,Eswaramoorthy, S.
Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B.
Nat.Struct.Biol., 7:693-699, 2000

PubMed Abstract: Clostridium botulinum neurotoxins are among the most potent toxins to humans. The crystal structures of intact C. botulinum neurotoxin type B (BoNT/B) and its complex with sialyllactose, determined at 1. 8 and 2.6 A resolution, respectively, provide insight into its catalytic and binding sites. The position of the belt region in BoNT/B is different from that in BoNT/A; this observation presents interesting possibilities for designing specific inhibitors that could be used to block the activity of this neurotoxin. The structures of BoNT/B and its complex with sialyllactose provide a detailed description of the active site and a model for interactions between the toxin and its cell surface receptor. The latter may provide valuable information for recombinant vaccine development.

PubMed: 10932256
DOI: 10.1038/78005

Experimental method

X-RAY DIFFRACTION (2.6 Å)