Structure of the full‐length insecticidal protein  C ry1 A c reveals intriguing details of toxin packaging into  in vivo  formed crystals | Zendy

Evdokimov Artem G. | Zendy; Moshiri Farhad | Zendy; Sturman Eric J. | Zendy; Rydel Timothy J. | Zendy; Zheng Meiying | Zendy; Seale Jeffrey W. | Zendy; Franklin Sonya | Zendy

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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) - toxin , in vivo , chemistry , microbiology and biotechnology , biophysics , biology , biochemistry , genetics

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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