3BTA
CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A
Summary for 3BTA
| Entry DOI | 10.2210/pdb3bta/pdb |
| Descriptor | PROTEIN (BOTULINUM NEUROTOXIN TYPE A), ZINC ION (2 entities in total) |
| Functional Keywords | neurotoxin, zinc protease, sugar binding protein, translocation, toxin |
| Biological source | Clostridium botulinum |
| Cellular location | Botulinum neurotoxin A light chain: Secreted. Botulinum neurotoxin A heavy chain: Secreted: P10845 |
| Total number of polymer chains | 1 |
| Total formula weight | 149545.22 |
| Authors | Stevens, R.C.,Lacy, D.B. (deposition date: 1998-08-12, release date: 1999-10-01, Last modification date: 2024-10-30) |
| Primary citation | Lacy, D.B.,Tepp, W.,Cohen, A.C.,DasGupta, B.R.,Stevens, R.C. Crystal structure of botulinum neurotoxin type A and implications for toxicity. Nat.Struct.Biol., 5:898-902, 1998 Cited by PubMed Abstract: Botulinum neurotoxin type A (BoNT/A) is the potent disease agent in botulism, a potential biological weapon and an effective therapeutic drug for involuntary muscle disorders. The crystal structure of the entire 1,285 amino acid di-chain neurotoxin was determined at 3.3 A resolution. The structure reveals that the translocation domain contains a central pair of alpha-helices 105 A long and a approximately 50 residue loop or belt that wraps around the catalytic domain. This belt partially occludes a large channel leading to a buried, negative active site--a feature that calls for radically different inhibitor design strategies from those currently used. The fold of the translocation domain suggests a mechanism of pore formation different from other toxins. Lastly, the toxin appears as a hybrid of varied structural motifs and suggests a modular assembly of functional subunits to yield pathogenesis. PubMed: 9783750DOI: 10.1038/2338 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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