Evidence map›Paper›PMID 24426173›Full record

ArticleIndian journal of microbiology2014

Insilico Structural 3D Modelling of Novel Cry1Ib9 and Cry3A Toxins from Local Isolates of Bacillus thuringiensis.

H M Mahadeva Swamy, R Asokan, Riaz Mahmood

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Article in Indian journal of microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

H M Mahadeva SwamyBio-Pesticide Laboratory (BPL), Division of Biotechnology, Indian Institute of Horticultural Research (IIHR), Hessarghatta Lake Post, Bangalore, 560089 India.
R AsokanBio-Pesticide Laboratory (BPL), Division of Biotechnology, Indian Institute of Horticultural Research (IIHR), Hessarghatta Lake Post, Bangalore, 560089 India.
Riaz MahmoodPost-Graduate Department of Studies and Research in Biotechnology and Bioinformatics, Kuvempu University, Jnanasahayadri, Shankaraghatta, Shimoga, 577451 Karnataka India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Three-dimensional (3D) models for the 79.2 kDa activated Cry1Ib9 and 77.4 kDa activated Cry3A δ-endotoxins from Bacillus thuringiensis (Bt) native isolates that are specifically toxic to Coleopteran insect pests were constructed by utilizing homology modeling online tool. Evidences presented here, based on the identification of structural equivalent residues of Cry1Ib9 and Cry3A toxin through homology modelling indicate that, they share a common Bt toxin tridimensional structure. The main differences observed in Cry1I9 domain I at positions α2b (S56-I60), α4 (F78-l93) and additionally β0 (Q10-L12), α8a (T280-V282) were observed, in domain II at positions α9b (P333-L339), β6(T390-Q393), β7(V398-W404), β8 (V418-W425), β9 (E453-N454), β10 (S470-I479) where as in domain III the changes were observed at positions β19 (R601-F607), β20 (609-L613), β21 (S618-F627) and α11a (K655-F664), α13, α14 components present at downstream sites, where as in Cry3A main differences observed in domain I is at the position of α4 (P105-I152), α5 (Q163-A185), β1A(E190-L192), α6 (F193-Y217), Domain II is not consevered and main variations were observed at β2 (E292-L295), β3(V299-L308), β4(I340-F347), β5(D356-P368), β6(I375-T377), β7(V389-F394), β8(K398-N405), β9(Y416-Y427), β10 (T436-Y439), β12(G476-H495), β12A (M503-I504) where as in domain III main variations observed at positions of β18 (P583-I593), β19(F604-S610), β20(P611-L615), β21(N619-G626). Cry1Ib9 and Cry3A contain the most variable regions in the loops of domain II, which determine the specificity of these toxins. These are the first models of Coleopteran-active protein from native isolates of Bt and its importance can be perceived since members of this group of toxins are potentially important candidates for coleoptera insect pest control programs.

Indexed as

3D ModelBacillus thuringiensisColeopteran-activeDisulfide bondHomology modelingδ-Endotoxin

Identifiers

PMID24426173
PMCPMC3889857

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.