Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals.

Autor: Evdokimov AG; Monsanto, GG4D 700 Chesterfield Parkway West, Chesterfield, Missouri, 63017., Moshiri F, Sturman EJ, Rydel TJ, Zheng M, Seale JW, Franklin S
Jazyk: angličtina
Zdroj: Protein science : a publication of the Protein Society [Protein Sci] 2014 Nov; Vol. 23 (11), pp. 1491-7. Date of Electronic Publication: 2014 Sep 02.
DOI: 10.1002/pro.2536
Abstrakt: 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.)
Databáze: MEDLINE
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