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Structure of the full‐length insecticidal protein C ry1 A c reveals intriguing details of toxin packaging into in vivo formed crystals
Author(s) -
Evdokimov Artem G.,
Moshiri Farhad,
Sturman Eric J.,
Rydel Timothy J.,
Zheng Meiying,
Seale Jeffrey W.,
Franklin Sonya
Publication year - 2014
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2536
Subject(s) - bacillus thuringiensis , cry1ac , toxin , enhancer , crystal structure , chemistry , in vivo , biophysics , crystallography , biology , biochemistry , bacteria , microbiology and biotechnology , genetics , genetically modified crops , transgene , gene , gene expression
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.