Format

Send to

Choose Destination
See comment in PubMed Commons below
Nat Struct Biol. 1998 Oct;5(10):898-902.

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

Author information

1
Department of Chemistry and Earnest Orlando Lawrence Berkeley National Laboratory, University of California, Berkeley, 94720, USA.

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.

PMID:
9783750
DOI:
10.1038/2338
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Nature Publishing Group
    Loading ...
    Support Center