3BTA

Crystal structure of botulinum neurotoxin type A and implications for toxicity.

(1998) Nat Struct Biol 5: 898-902

• PubMed: 9783750 Search on PubMed
• DOI: https://doi.org/10.1038/2338
• Primary Citation of Related Structures:  
  3BTA


• 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.

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Organizational Affiliation: 

Department of Chemistry and Earnest Orlando Lawrence Berkeley National Laboratory, University of California, Berkeley, 94720, USA.