Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging intoin vivoformed crystals

Autor:	Artem G. Evdokimov, Timothy J. Rydel, Sonya J. Franklin, Meiying Zheng, Jeffrey W. Seale, Farhad Moshiri, Eric J. Sturman
Rok vydání:	2014
Předmět:	Stereochemistry Toxin fungi Biology biology.organism_classification medicine.disease_cause Biochemistry Crystal Protein structure Cry1Ac In vivo Bacillus thuringiensis Biophysics medicine Natural enemies Enhancer Molecular Biology
Zdroj:	Protein Science. 23:1491-1497
ISSN:	0961-8368
Popis:	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.
Databáze:	OpenAIRE
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