The role of a proline-induced broken-helix motif in alpha-helix 2 of Bacillus thuringiensis delta-endotoxins |
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Authors: | Arnold S Curtiss A Dean D H Alzate O |
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Affiliation: | Molecular Genetics Department, The Ohio State University, 484 W. 12th Ave., Columbus, OH 43210-1292, USA. |
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Abstract: | Bacillus thuringiensis delta-endotoxins (Cry proteins), are widely used for insect control and plant protection. They are water-soluble proteins that insert into membranes forming ion channels. In most Cry toxins alpha-helix 2 is broken by a highly conserved proline residue (Pro70 in Cry1Ab), generating a broken-helix motif. The flexibility of the motif was altered through site-directed mutagenesis. It was found that increasing the flexibility of the motif decreased the stability, the ion transport ability and the toxicity of the protein. By removing the broken-helix motif, the biological properties were restored to a wild type level. |
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