7Y78

Crystal structure of Cry78Aa

7Y78 の概要

• エントリーDOI: 10.2210/pdb7y78/pdb
• 分子名称: Toxin, AMMONIUM ION, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: cry78aa, plant hopper, toxin
• 由来する生物種: Bacillus thuringiensis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 159498.72

構造登録者

Cao, B.B.,Nie, Y.F.,Wang, N.C.,Guan, Z.Y.,Zhang, D.L.,Zhang, J. (登録日: 2022-06-21, 公開日: 2022-08-31, 最終更新日: 2024-05-29)

主引用文献

Cao, B.,Nie, Y.,Guan, Z.,Chen, C.,Wang, N.,Wang, Z.,Shu, C.,Zhang, J.,Zhang, D.
The crystal structure of Cry78Aa from Bacillus thuringiensis provides insights into its insecticidal activity.
Commun Biol, 5:801-801, 2022

PubMed Abstract: Genetically modified plants with insecticidal proteins from Bacillus thuringiensis (Bt) have been successfully utilized to control various kinds of pests in crop production and reduce the abuse of pesticides. However, a limited number of genes are available for the protection of crops from rice planthopper. Recently, Cry78Aa protein from Bt strain C9F1 has been found to have high insecticidal activity against Laodelphax striatellus and Nilaparvata lugens. It is the first reported single-component protein in the world to combat rice planthoppers, making it very promising for use in transgenic crops. The ambiguous mechanism of Cry78Aa functions prevented further engineering or application. Here, we report the crystal structure of Cry78Aa, which consists of two domains: a C-terminal β-pore forming domain belonging to the aerolysin family and an N-terminal trefoil domain resembling the S-type ricin B lectin. Thus, Cry78Aa could represent a distinctive type of β-pore forming toxin. We also found that Cry78Aa binds carbohydrates such as galactose derivatives and is essential for insecticidal activity against Laodelphax striatellus. Our results suggest a mechanism underlying the function of Cry78Aa against rice planthoppers and pave the way to maximizing the usage of the toxin.

PubMed: 35945427
DOI: 10.1038/s42003-022-03754-6

実験手法

X-RAY DIFFRACTION (2.9 Å)