Three-Dimensional Structure Determination of Botulinum Toxin.

Abstract

The immediate goals of the contract on the structure and function relationship of botulinum neurotoxin are: 1) Determine the three-dimensional structure of botulinum neurotoxin at atomic resolution by x-ray crystallography. 2) Based on the structure of the neurotoxin, understand the toxins mechanism of action. We have accomplished the first goal of determining the three-dimensional structure of the 150 kD botulinum neurotoxin serotype A. The toxin is Y-shaped, with a very long alpha-helical translocation domain forming the backbone of the structure. The translocation domain is composed almost entirely of helices, 2 of which are 9s A in length and form a pseudo-coiled coil. The binding domain and catalytic domain are more globular in shape, located at two different ends of the translocation domain. The overall dimensions of the protein are 120 A x 80 A x 40 A. A complete description of the three- dimensional structure is described in the report. Refinement and analysis of the structure are presently in progress.

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Document Details

Document Type
Technical Report
Publication Date
May 01, 1997
Accession Number
ADA328904

Entities

People

  • Ray C. Stevens

Organizations

  • University of California

Tags

DTIC Thesaurus Topics

  • Amino Acids
  • Biomedical And Dental Materials
  • Cells
  • Chemical Reactions
  • Chemical Synthesis
  • Chemistry
  • Crystal Structure
  • Crystallography
  • Crystals
  • Electron Density
  • Materials
  • Medical Personnel
  • Synapses
  • Three Dimensional
  • X Rays
  • X-Ray Crystallography

Fields of Study

  • Chemistry

Readers

  • Computational Fluid Dynamics (CFD)
  • Molecular and Cellular Biochemistry