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

Nature volume 353, pages 815–821 (1991)Cite this article

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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Authors and Affiliations

  1. Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Jade Li

  2. Biochemistry Department, Cambridge University, Tennis Court Road, Cambridge, CB2 1QW, UK

    Joe Carroll & David J. Ellar

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  1. Jade Li
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  2. Joe Carroll
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  3. David J. Ellar
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Li, J., Carroll, J. & Ellar, D. Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution. Nature 353, 815–821 (1991). https://doi.org/10.1038/353815a0

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