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Figure 8 | BMC Biochemistry

Figure 8

From: Ser170 of Bacillus thuringiensis Cry1Ab δ-endotoxin becomes anchored in a hydrophobic moiety upon insertion of this protein into Manduca sexta brush border membranes

Figure 8

Model of the membrane-bound α-Helix 5. The structural transformation suggested by the use of spin-labelled α-helix 5, indicates that this helix participates asymmetrically in the ion channel activity of the toxin. In the membrane-bound state Ser176 is part of the ion pore, while Leu157 is not. In contrast, amino acid Ser170 changes from a mobile to a less-mobile conformation.

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BMC Biochemistry

ISSN: 1471-2091

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