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

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...

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Bibliographic Details
Published inProtein science Vol. 23; no. 11; pp. 1491 - 1497
Main Authors Evdokimov, Artem G., Moshiri, Farhad, Sturman, Eric J., Rydel, Timothy J., Zheng, Meiying, Seale, Jeffrey W., Franklin, Sonya
Format Journal Article
LanguageEnglish
Published United States Wiley Subscription Services, Inc 01.11.2014
BlackWell Publishing Ltd
Subjects
Accelerated Communication
Bacillus thuringiensis
Bacillus thuringiensis Toxins
Bacterial Proteins - chemistry
Biocompatibility
Cry1A
Cry1Ac toxin
Crystal structure
Crystals
Endotoxins - chemistry
Hemolysin Proteins - chemistry
insecticidal toxin
insecticidal toxin mode of action
Insecticides - chemistry
Models, Molecular
natural crystal packing
Packaging
Protein Conformation
Proteins
Recombinant Proteins - chemistry
structure of full length toxin
structure of full length toxin
insecticidal toxin mode of action
natural crystal packing
Bacillus thuringiensis
insecticidal toxin
Cry1A
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Summary: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. Interactive Figure 2; Interactive Figure 4
Bibliography:Artem Evdokimov and Farhad Moshiri contributed equally to this work.
Conflict of interest statement: authors would like to declare that this work has been performed as a part of a broader commercial interest into ongoing studies of insecticidal proteins.
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.2536