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J Mol Model. 2008 Sep;14(9):843-8. doi: 10.1007/s00894-008-0318-8. Epub 2008 May 27.

The theoretical 3D structure of Bacillus thuringiensis Cry5Ba.

Author information

1
Key Laboratory for Microbial Molecular Biology of Hunan Province, College of Life Science, Hunan Normal University, Changsha 410081, China. xialq@hunnu.edu.cn

Abstract

Cry5Ba is a delta-endotoxin produced by Bacillus thuringiensis PS86A1 NRRL B-18900. It is active against nematodes and has great potential for nematode control. Here, we predict the first theoretical model of the three-dimensional (3D) structure of a Cry5Ba toxin by homology modeling on the structure of the Cry1Aa toxin, which is specific to Lepidopteran insects. Cry5Ba resembles the previously reported Cry1Aa toxin structure in that they share a common 3D structure with three domains, but there are some distinctions, with the main differences being located in the loops of domain I. Cry5Ba exhibits a changeable extending conformation structure, and this special structure may also be involved in pore-forming and specificity determination. A fuller understanding of the 3D structure will be helpful in the design of mutagenesis experiments aimed at improving toxicity, and lead to a deep understanding of the mechanism of action of nematicidal toxins.

PMID:
18504623
DOI:
10.1007/s00894-008-0318-8
[Indexed for MEDLINE]

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