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Abstract

ABSTRACT:We predict the first theoretical structural model of the newly reported Cry1Ab17 δ-endotoxin produced by Bacillus thuringiensis using homology modelling. Both Cry1Ab17 and Cry1Aa share a common structure; both contain three flexible domains that participate in the formation of a pore and determine the receptor binding specificity. The main differences between the two is in the length of loops, and in Cry1Ab17, the absence of α7b, α10a, α10b, α12a, β19, β20 and presence of additional β0 β1b, α9b components. A few of the components such as α8a, α8b, α9a, α9b, and α11a differ in their locations. A better understanding of the 3-D structure of Cry1Ab17 will be helpful in designing the domain swapping experiments to improve its insecticidal toxicity.