publication . Article . 2001

The role of a proline‐induced broken‐helix motif in α‐helix 2 of Bacillus thuringiensis δ‐endotoxins

Suzanne Arnold; April Curtiss; Donald H. Dean; Oscar Alzate;
Open Access English
  • Published: 09 Feb 2001 Journal: FEBS Letters, issue 1-2, pages 70-74 (issn: 00145793, Copyright policy)
  • Publisher: Federation of European Biochemical Societies. Published by Elsevier B.V.
AbstractBacillus thuringiensis δ-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 α-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.
free text keywords: Cry protein, δ-Endotoxin, Endotoxin, Bacillus thuringiensis, Biophysics, Genetics, Cell Biology, Biochemistry, Molecular Biology, Structural Biology, Ion channel, Membrane, Proline, Helix, Wild type, biology.organism_classification, biology, Mutagenesis, Ion transporter
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