Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution

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Abstract
The structure of the δ-endotoxin from Bacillus thuringiensis subsp. tenebrionis that is specifically toxic to Coleopterajnsects (beetle toxin) has been determined at 2.5 Å resolution. It comprises three domains which are, from the N- to C-termini, a seven-helix bundle, a three-sheet domain, and a β sandwich. The core of the molecule encompassing all the domain interfaces is built from conserved sequence segments of the active δ-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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