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Mahadeva Swamy, H.M.
- Homology Modeling Deduced Tridimensional Structure of Novel Coleopteran Bacillus Thuringiensis Cry1ib8 Toxin and in Silicon Analysis
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Authors
Affiliations
1 Bio-Pesticide Laboratory, Division of Biotechnology, Indian Institute of Horticultural Research (IIHR), Hessarghatta Lake Post, Bangalore 560 089, IN
2 Bio-Pesticide laboratory (BPL), Division of Biotechnology, Indian Institute of Horticultural Research (IIHR), Hessarghatta lake post, Bangalore 560 089, IN
3 2Post-Graduate Department of Studies and Research in Biotechnology and Bioinformatics, Kuvempu University, Jnanasahayadri, Shankaraghatta, Shimoga 577451, Karnataka, IN
1 Bio-Pesticide Laboratory, Division of Biotechnology, Indian Institute of Horticultural Research (IIHR), Hessarghatta Lake Post, Bangalore 560 089, IN
2 Bio-Pesticide laboratory (BPL), Division of Biotechnology, Indian Institute of Horticultural Research (IIHR), Hessarghatta lake post, Bangalore 560 089, IN
3 2Post-Graduate Department of Studies and Research in Biotechnology and Bioinformatics, Kuvempu University, Jnanasahayadri, Shankaraghatta, Shimoga 577451, Karnataka, IN
Source
Indian Journal of Biotechnology & Biochemistry, Vol 1, No 1 (2013), Pagination: 37-56Abstract
Cry1I toxins are particularly interesting from an agricultural perspective because of their wide host range. We presented 3D structural model of the novel Coleopteran active Cry1Ib8 δ-endotoxin obtained from native Bt strain using homology modeling. Cry1Ib8 share a common structure contains three flexible domains that participate in the formation of a pore and determine the receptor binding specificity. The pore-forming domain I is composed of residues 60-282. It consists of 10α-helices and two small β-strands. The identified helices and strands are as follows: α1 (E33-K35); α2a (N39-S46); α2b (S56-I60); α3 (Q61-T73); α4 (F78-L93); α5 (K98- V146); α6 (T152-F177); α7a (L185-W210); α7b (A214-L246); α8a (T280-V282); β0 (Q10-L12) and β1a (E182-P184). Domain II comprised of residues 287-487, two helix (α9 F322-A328; α10 P333- L339) and 10 β-strands (β2 T292-T297; β3 V342-S346; β4 M359- P369; β5- L374-N375; β6 T390-Q393; β7 V398-W404; β9 E453- N454; β10 S470-I479 and β11 A486-H493). Domain III is comprised of residues 507-644, has a three antiparallel-sheet sandwich structure present at downstream sites (α11a K655-F664; α13 E678-S690; α14 L697-R718 and α12a is absent) and shows highly conserved β residues. Understanding the mode of action of coleopteran-specific B. thuringiensis toxins through 3-D homology models will aid in the development of novel B. thuringiensis biopesticide with increased efficacy as well as in the development of resistance detection and management strategies.Keywords
3D Structure, Domains, Homology Modeling, Native Bt Strains
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