1EPW
CRYSTAL STRUCTURE OF CLOSTRIDIUM NEUROTOXIN TYPE B
Summary for 1EPW
| Entry DOI | 10.2210/pdb1epw/pdb |
| Descriptor | BOTULINUM NEUROTOXIN TYPE B, ZINC ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | botulinum, zinc, metalloprotease, transmembrane, neurotoxin, 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 | 150994.85 |
| Authors | Swaminathan, S.,Eswaramoorthy, S. (deposition date: 2000-03-29, 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 Cited by 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: 10932256DOI: 10.1038/78005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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