Three Dimensional Structure Determination of Botulinum Neurotoxin
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 95 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 also included. To date, a total of 8 manuscripts have been published, and 3 Ph.D. thesis generated.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 1999
- Accession Number
- ADA368202
Entities
People
- Raymond C. Stevens
Organizations
- University of California, Berkeley