7y78 | pdb_00007y78
Crystal structure of Cry78Aa
Structural highlights
FunctionPublication Abstract from PubMedGenetically 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 beta-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 beta-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. The crystal structure of Cry78Aa from Bacillus thuringiensis provides insights into its insecticidal activity.,Cao B, Nie Y, Guan Z, Chen C, Wang N, Wang Z, Shu C, Zhang J, Zhang D Commun Biol. 2022 Aug 9;5(1):801. doi: 10.1038/s42003-022-03754-6. PMID:35945427[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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