[Structural changes in Cry3A delta-endotoxin from Bacillus thuringiensis var. Tenebrionis in alcohol solutions at pH 2.0]

Biofizika. 2005 Jan-Feb;50(1):28-38.
[Article in Russian]

Abstract

Conformational changes in Cry3A delta-endotoxin caused by three different alcohols (ethanol, butanol, and isopropanol) were studied using the methods of circular dichroism, scanning microcalorimetry, and electron miscroscopy. It was shown that, in addition to the standard decrease in the native structure stability, the alcohols can cause a conformational transition that results in a sharp increase in the beta-structure content and a change in the environment of aromatic residues. The conformational transition is accompanied by intermolecular association, which leads to the appearance of oligomers in the form of short filaments. When the alcohols were removed, the oligomers dissociated again into monomers, but it is likely that the native structure either is not restored or is restored only in a small portion of molecules. The oligomer structure is rather cooperative, and its thermostability is higher than that of the initial structure. The disruption of this structure upon heating, observed as a heat absorption peak, is reversible.

MeSH terms

  • Alcohols / chemistry*
  • Bacillus thuringiensis / chemistry*
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / ultrastructure
  • Bacterial Toxins / chemistry*
  • Calorimetry, Differential Scanning
  • Circular Dichroism
  • Electrophoresis, Polyacrylamide Gel
  • Endotoxins / chemistry*
  • Hemolysin Proteins
  • Hydrogen-Ion Concentration*
  • Hydrolysis
  • Microscopy, Electron
  • Protein Conformation

Substances

  • Alcohols
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Bacterial Toxins
  • Endotoxins
  • Hemolysin Proteins
  • insecticidal crystal protein, Bacillus Thuringiensis