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The theoretical homology based structural model of Cry1Ab15   δ  -endotoxin produced by  Bacillus thuringiensis  BtB-Hm-16 was predicted using the Cry1Aa template (resolution 2.25 Å). The Cry1Ab15 resembles the template structure by sharing a common three-domain extending conformation structure responsible for pore-forming and specificity determination. The novel structural differences found are the presence of   β  0 and   α  3, and the absence of   α  7b,   β  1a,   α  10a,   α  10b,   β  12, and   α  11a while   α  9 is located spatially downstream. Validation by SUPERPOSE and with the use of PROCHECK program showed folding of 98% of modeled residues in a favourable and stable orientation with a total energy  Z -score of −6.56; the constructed model has an RMSD of only 1.15 Å. These increments of 3D structure information will be helpful in the design of domain swapping experiments aimed at improving toxicity and will help in elucidating the common mechanism of toxin action.

In SilicoModeling and Functional Interpretations of Cry1Ab15 Toxin fromBacillus thuringiensisBtB-Hm-16