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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...

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Identifiers

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

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The alpha-helix 4 residue, Asn135, is involved in the oligomerization of Cry1Ac1 and Cry1Ab5 Bacillus thuringiensis toxins.PMID 11722927Read ↗

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