title: Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals.
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.
authors.affiliation: Monsanto, GG4D 700 Chesterfield Parkway West, Chesterfield, Missouri, 63017.
authors.forename: Artem G
authors.initials: AG
authors.lastname: Evdokimov
authors.forename: Farhad
authors.initials: F
authors.lastname: Moshiri
authors.forename: Eric J
authors.initials: EJ
authors.lastname: Sturman
authors.forename: Timothy J
authors.initials: TJ
authors.lastname: Rydel
authors.forename: Meiying
authors.initials: M
authors.lastname: Zheng
authors.forename: Jeffrey W
authors.initials: JW
authors.lastname: Seale
authors.forename: Sonya
authors.initials: S
authors.lastname: Franklin
mesh_terms: D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000737:chemistry*; D004731:Endotoxins / Q000737:chemistry*; D006460:Hemolysin Proteins / Q000737:chemistry*; D007306:Insecticides / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D004731:Endotoxins; D006460:Hemolysin Proteins; D007306:Insecticides; D011994:Recombinant Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis
keywords: Bacillus thuringiensis; Cry1A; insecticidal toxin; insecticidal toxin mode of action; natural crystal packing; structure of full length toxin