Molecular modeling and characterization of the B. thuringiensis and B. thuringiensis LDC-9 cytolytic proteins.
J Biomol Struct Dyn, 2008/12;26(3):375-86.
Mahalakshmi A[1], Sujatha K, Shenbagarathai R
Affiliations
PMID: 18808203
Impact factor: 5.235
Abstract
The Cyt toxins are able to lyse a wide range of cell types in vitro, unlike the Cry delta-endotoxins. It exerts its activity by the formation of pores within target cell membranes. The structural information available for Cyt2Aa (PDB id: 1CBY) consists of a single domain in which two outer layers of alpha-helix wrap around a mixed beta-sheet. Beta-barrel was suggested as a possible structure of the pores. Hence, this study seeks to investigate the structural properties of other Cytolytic proteins by predicting the three-dimensional (3D) model using Cyt2Aa as template. The predicted models are expected to be significantly more accurate as all the Cyt proteins showed significant similarity with the template (PDB id: 1CBY). The refined homology models revealed similar secondary structures (alpha-helices and beta-sheets) and tertiary features as Cyt2Aa. The variation in the loop regions of the tertiary structure accounts for the differential toxicity.
MeSH terms
Amino Acid Sequence; Bacillus thuringiensis; Bacterial Proteins; Computer Simulation; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment
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