What question did this study set out to answer?

Determine the three-dimensional crystal structure of the coleopteran-active delta-endotoxin Cry3Bb1 to understand its insecticidal mechanism and specificity.

July 23, 2001Acta Crystallographica Section D Biological Crystallography

Structure of the insecticidal bacterial δ-endotoxin Cry3Bb1 ofBacillus thuringiensis

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Authors

NGNikolai GalitskyHauptman-Woodward Medical Research Institute VCVivian CodyHauptman-Woodward Medical Research Institute AWAndrzej WojtczakNicolaus Copernicus University

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Implication

Structural analysis uncovers a dimeric three-domain architecture in Bacillus thuringiensis Cry3Bb1 toxin, suggesting mechanisms behind target pest specificity.

Key Points

Determine the three-dimensional crystal structure of the coleopteran-active delta-endotoxin Cry3Bb1 to understand its insecticidal mechanism and specificity.
Refined the X-ray crystal structure of the delta-endotoxin Cry3Bb1 from Bacillus thuringiensis strain EG7231 using diffraction data collected to 2.4 Å resolution.
Analyzed domain organization and inter-monomer interactions across a crystallographic twofold axis in an orthorhombic C222(1) crystal lattice.
The structure was refined to a residual R factor of 17.5% and R(free) of 25.3%, revealing three domains: a seven-helix bundle (I), a three-sheet domain (II), and a beta-sandwich domain (III).
Cry3Bb1 forms a stable dimer via 23 inter-monomer hydrogen bonds and a channel composed of domains I and III, providing a structural basis for oligomerization in solution.
Comparison with the Cry3A toxin identified seven extra amino acid residues, primarily within domain III, which corresponds to the largest conformational variation and likely dictates pest selectivity.

Cite This Study

Galitsky et al. (2001) studied this question.

synapsesocial.com/papers/6a98ea44102402788c361bb2 https://doi.org/10.1107/s0907444901008186

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Implication

Structural analysis uncovers a dimeric three-domain architecture in Bacillus thuringiensis Cry3Bb1 toxin, suggesting mechanisms behind target pest specificity.

Structure of the insecticidal bacterial δ-endotoxin Cry3Bb1 ofBacillus thuringiensis

Discussion

Member takes

Implication

Key Points

Cite This Study

Structure of the insecticidal bacterial δ-endotoxin Cry3Bb1 ofBacillus thuringiensis

Discussion

Member takes

Implication

Key Points

Cite This Study

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