The Structure of the Neurotoxin- Associated Protein HA33/A from Clostridium botulinum Suggests a Reoccurring Beta-Trefoil Fold in the Progenitor Toxin Complex

Abstract

The hemagglutinating protein HA33 from Clostridium botulinum is associated with the large botulinum neurotoxin secreted complexes and is critical in toxin protection, internalization, and possibly activation. We report the crystal structure of serotype A HA33 (HA33/A) at 1.5 A resolution that contains a unique domain organization and a carbohydrate recognition site. In addition, sequence alignments of the other toxin complex components, including the neurotoxin BoNT/A, hemagglutinating protein HA17/A, and non-toxic non-hemagglutinating protein NTNHA/A, suggests that most of the toxin complex consists of a reoccurring beta-trefoil fold.

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Document Details

Document Type
Technical Report
Publication Date
Dec 16, 2004
Accession Number
ADA434669

Entities

People

  • Frank L. Lebeda
  • Jenny Gu
  • Joseph W. Arndt
  • Lukasz Jaroszewski
  • Michael A. Hanson
  • Raymond C. Stevens
  • Robert Schwarzenbacher

Organizations

  • United States Army Medical Research Institute of Infectious Diseases

Tags

DTIC Thesaurus Topics

  • Biology
  • Carbohydrates
  • Cells
  • Chemistry
  • Clostridium
  • Crystal Structure
  • Crystals
  • Identification
  • Molecular Biology
  • Molecules
  • Neurotoxins
  • Recognition
  • Sequences
  • Statistics
  • Synapses
  • Toxins
  • X Rays

Fields of Study

  • Biology
  • Chemistry

Readers

  • Microbial Pathology
  • Molecular and Cellular Biochemistry