Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals.
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ABSTRACT:
SUBMITTER: Evdokimov AG
PROVIDER: S-EPMC4241100 | biostudies-literature | 2014 Nov
REPOSITORIES: biostudies-literature
Publications
Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals.
Evdokimov Artem G AG Moshiri Farhad F Sturman Eric J EJ Rydel Timothy J TJ Zheng Meiying M Seale Jeffrey W JW Franklin Sonya S
Protein science : a publication of the Protein Society 20140902 11
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. ...[more]
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