Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals.
Protein Sci
; 23(11): 1491-7, 2014 Nov.
Article
em En
| MEDLINE
| ID: mdl-25139047
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.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Endotoxinas
/
Proteínas Hemolisinas
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Inseticidas
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article