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Figure 1 | BMC Biochemistry

Figure 1

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 1

Three-dimensional representation of B. thuringiensis Cry1Ab δ-endotoxin showing the mutations introduced in α-Helix 5 (black in the figure). L157 is located at the N-terminal end of the helix (red spheres), S170 in the middle of the helix (blue spheres) and S176 at the C-terminal end (green spheres). The inset shows a view of the toxin from top of the α-helical domain to indicate the central location and the orientation of the amino acid residues mutated for this study.

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BMC Biochemistry

ISSN: 1471-2091

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