Crystal structure of insecticidal delta-endotoxin from Bacillus thuringiensis at 2.5 angstroms resolution
1991
Li, J. | Carroll, J. | Ellar, D.J.
The structure of the delta-endotoxin from Bacillus thuringiensis subsp. tenebrionis that is specifically toxic to Coleoptera insects (beetle toxin) has been determined at 2.5 angstroms resolution. It comparises three domains which are, from the N- to C-termini, a seven-helix bundle, a three-sheet domain, and a beta sandwich. The core of the molecule encompassing all the domain interfaces is built from conserved sequence segments of the active delta-endotoxins. Therefore the structure represents the general fold of this family of insecticidal proteins. The bundle of long, hydrophobic and amphipathic helices is equipped for pore formation in the insect membrane and regions of the three-sheet domain are probably responsible for receptor binding.
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