| Literature DB >> 25139047 |
Artem G Evdokimov1, Farhad Moshiri, Eric J Sturman, Timothy J Rydel, Meiying Zheng, Jeffrey W Seale, Sonya Franklin.
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.Entities:
Keywords: Bacillus thuringiensis; Cry1A; insecticidal toxin; insecticidal toxin mode of action; natural crystal packing; structure of full length toxin
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Year: 2014 PMID: 25139047 PMCID: PMC4241100 DOI: 10.1002/pro.2536
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725