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Homology Modeling of Cyt2Ca1 of Bacillus thuringiensis and Its Molecular Docking with Inositol Monophosphate
Author(s) -
Zhao Xinming,
Xia Liqiu,
Ding Xuezhi,
Yu Ziquan,
LÜ Yuan,
Tao Wenna
Publication year - 2009
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200990350
Subject(s) - bacillus thuringiensis , homology modeling , chemistry , docking (animal) , stereochemistry , molecular model , biochemistry , sulfonylurea , toxin , enzyme , biology , genetics , bacteria , medicine , nursing , insulin , endocrinology
Cyt2Ca1 is an insecticidal crystal protein produced by Bacillus thuringiensis ET29 during its stationary phase, and this δ‐endotoxin demonstrates remarkable insecticidal activity against not only insects of the order Coleoptera , but also against fleas, and in particular the larvae of the cat flea, Ctenocephalides felis . The first theoretical model of the three‐dimensional structure of Cyt2Ca1 was predicted and compared with Cyt2Aa, which is lethal to insect larvae. The three‐dimensional structure of the Cyt2Ca1 was obtained by homology modeling on the structures of the Cyt2Aa protein. The deduced model resembles previously reported Cyt2Aa toxin. A binding mode of inositol monophosphate as a polar head group of the putative membrane phospholipid ligand to Cyt2Ca1 was presented using molecular docking. The residues of Leu9, Glu21, Tyr23 and Gln110 of the Cyt2Ca1 toxin are responsible for the interactions with inositol monophosphate via eight hydrogen bonds. Those residues could be important for receptor recognition. This binding simulation will be helpful for the design of mutagenesis experiments aimed at the improvement of toxicity, and lead to a deep understanding of the mechanism of action of Cyt toxins.