Lipid-induced conformation of helix 7 from the pore-forming domain of the Bacillus thuringiensis Cry4Ba toxin: implications for toxicity mechanism.

@article{Tiewsiri2009LipidinducedCO,
  title={Lipid-induced conformation of helix 7 from the pore-forming domain of the Bacillus thuringiensis Cry4Ba toxin: implications for toxicity mechanism.},
  author={Kasorn Tiewsiri and Wolfgang B. Fischer and Chanan Angsuthanasombat},
  journal={Archives of biochemistry and biophysics},
  year={2009},
  volume={482 1-2},
  pages={
          17-24
        }
}
Helix 7 in the Cry4Ba-pore-forming domain contains conserved Tyr(249) and Phe(264) that are crucially involved in mosquito-larvicidal activity. We have now characterized lipid-induced conformation of a 27-residue Cry4Ba-alpha7 peptide in phospholipid membranes using ATR-FTIR and hydrogen/deuterium (H(+)/D(+)) exchange experiments. ATR-FTIR results showed that conformation of this peptide is influenced by lipid composition and peptide-lipid ratio. For zwitterionic membranes, 1,2-dimyristoyl-sn… CONTINUE READING

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