The alpha-helix 4 residue, Asn135, is involved in the oligomerization of Cry1Ac1 and Cry1Ab5 Bacillus thuringiensis toxins.

doi:10.1128/AEM.67.12.5715-5720.2001

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Article

The alpha-helix 4 residue, Asn135, is involved in the oligomerization of Cry1Ac1 and Cry1Ab5 Bacillus thuringiensis toxins.

Applied and environmental microbiology - 1 Dec 2001

Tigue N J, Jacoby J, Ellar D J

Abstract excerpt

The insecticidal Cry toxins produced by the bacterium Bacillus thuringiensis are comprised of three structural domains. Domain I, a seven-helix bundle, is thought to penetrate the insect epithelial cell plasma membrane through a hairpin composed of alpha-helices 4 and 5, followed by the oligomerization of four hairpin monomers. The alpha-helix 4 has been proposed to line the lumen of the pore, whereas some...

Topics

Animals
Bacillus thuringiensis
Bacillus thuringiensis Toxins
Bacterial Proteins
Bacterial Toxins
Cell Membrane
Cell Membrane Permeability
Endotoxins
Hemolysin Proteins
Manduca
Mutation

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Identifiers

PMID: 11722927
DOI: 10.1128/AEM.67.12.5715-5720.2001
PMCID: PMC93364

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