Bacillus thuringiensis Cry4A and Cry4B Mosquito-larvicidal Proteins: Homology-based 3D Model and Implications for Toxin Activity
Angsuthanasombat, Chanan;Uawithya, Panapat;Leetachewa, Somphob;Pornwiroon, Walairat;Ounjai, Puey;Katzenmeier, Gerd;Panyim, Sakol(Mahidol University, Salaya Campus, Nakornpathom, Thailand)E-mail:[email protected] | Kerdcharoen, Teerakiat(Mahidol University, Bangkok, Thailand)
Three-dimensional (3D) models for the 65-kDa activated Cry4A and Cry4B δ-endotoxins from Bacillus thuringiensis subsp. israelensis that are specifically toxic to mosquito-larvae were constructed by homology modeling, based on atomic coordinates of the Cry1Aa and Cry3Aa crystal structures. They were structurally similar to the known structures, both derived 3D models displayed a three-domain organization: the N-terminal domain (I) is a seven-helix bundle, while the middle and C-terminal domains are primarily comprise of anti-parallel β-sheets.
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