ArticleIndian journal of microbiology2012
Computational Modeling Deduced Three Dimensional Structure of Cry1Ab16 Toxin from Bacillus thuringiensis AC11.
Article in Indian journal of microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Peptide isolated from Cry1Ab16 toxin present in Bacillus thuringiensis: Synthesis and morphology data for layer-by-layer films studied by atomic force microscopy.Data in brief · 2016Article
- CryGetter: a tool to automate retrieval and analysis of Cry protein data.BMC bioinformatics · 2016Article
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Abstract
The first theoretical structural model of newly reported Cry1Ab16 δ-endotoxin produced by Bacillus thuringiensis AC11 was predicted using homology modeling technique. Cry1Ab16 resembles the Cry1Aa protein structure by sharing a common three domains structure responsible in pore forming and specificity determination along with few structural deviations. The main differences between the two is in the length of loops, absence of α7b, α9a, α10b, α11a and presence of additional β12b, α13 components while α10a is spatially located at downstream position in Cry1Ab16. A better understanding of the 3D structure shall be helpful in the design of domain swapping and mutagenesis experiments aimed at improving toxicity.
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