全长杀虫蛋白Cry1Ac的结构揭示了毒素包装到体内形成晶体的有趣细节。
Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals.
作者信息
Evdokimov Artem G, Moshiri Farhad, Sturman Eric J, Rydel Timothy J, Zheng Meiying, Seale Jeffrey W, Franklin Sonya
机构信息
Monsanto, GG4D 700 Chesterfield Parkway West, Chesterfield, Missouri, 63017.
出版信息
Protein Sci. 2014 Nov;23(11):1491-7. doi: 10.1002/pro.2536. Epub 2014 Sep 2.
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.
摘要
自1965年首次对苏云金芽孢杆菌（Bt）产生的晶体进行表征以来，近半个世纪里，全长Bt杀虫蛋白Cry1Ac的结构一直未被研究人员破解。在最终解析出该结构后，我们报告了该蛋白毒性核心与原毒素结构域之间基于晶格的相互作用的有趣细节。该结构为原毒素作为天然晶体堆积和稳定性增强剂的功能提供了确凿证据。
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