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Start Over Author "Sturman, Eric J." Journal protein science a publication of the protein society
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1. Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals.

Author

Evdokimov AG, Moshiri F, Sturman EJ, Rydel TJ, Zheng M, Seale JW, and Franklin S

Subjects
Bacillus thuringiensis Toxins, Models, Molecular, Protein Conformation, Recombinant Proteins chemistry, Bacterial Proteins chemistry, Endotoxins chemistry, Hemolysin Proteins chemistry, Insecticides chemistry
Abstract

For almost half a century, the structure of the full-length Bacillus thuringiensis (Bt) insecticidal protein Cry1Ac has eluded researchers, since Bt-derived crystals were first characterized in 1965. Having finally solved this structure we report intriguing details of the lattice-based interactions between the toxic core of the protein and the protoxin domains. The structure provides concrete evidence for the function of the protoxin as an enhancer of native crystal packing and stability., (© 2014 The Protein Society.)

Published
2014
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