7YP0

Crystal structure of CtGST

Summary for 7YP0

• Entry DOI: 10.2210/pdb7yp0/pdb
• Descriptor: Glutathione S-transferase (2 entities in total)
• Functional Keywords: deoxynivaneol detoxification enzyme, glutathione s-transferase, transferase
• Biological source: Colletotrichum tofieldiae
• Total number of polymer chains: 2
• Total formula weight: 62775.14

Authors

Yang, J.,Fan, J.P.,Lei, X.G. (deposition date: 2022-08-02, release date: 2024-02-07, Last modification date: 2024-03-13)

Primary citation

Yang, J.,Liang, K.,Ke, H.,Zhang, Y.,Meng, Q.,Gao, L.,Fan, J.,Li, G.,Zhou, H.,Xiao, J.,Lei, X.
Enzymatic Degradation of Deoxynivalenol with the Engineered Detoxification Enzyme Fhb7.
Jacs Au, 4:619-634, 2024

PubMed Abstract: In the era of global climate change, the increasingly severe head blight (FHB) and deoxynivalenol (DON) contamination have caused economic losses and brought food and feed safety concerns. Recently, an FHB resistance gene coding a glutathione-S transferase (GST) to degrade DON by opening the critical toxic epoxide moiety was identified and opened a new window for wheat breeding and DON detoxification. However, the poor stability of Fhb7 and the elusiveness of the catalytic mechanism hinder its practical application. Herein, we report the first structure of Fhb7 at 2.41 Å and reveal a unique catalytic mechanism of epoxide opening transformation in GST family proteins. Furthermore, variants V29P and M10 showed that 5.5-fold and 266.7-fold longer half-life time than wild-type, respectively, were identified. These variants offer broad substrate scope, and the engineered biosafe overexpressing the variants shows excellent DON degradation performance, exhibiting potential at bacterium engineering to achieve DON detoxification in the feed and biomedicine industry. This work provides a profound mechanistic insight into the enzymatic activities of Fhb7 and paves the way for further utilizing Fhb7-related enzymes in crop breeding and DON detoxification by synthetic biology.

PubMed: 38425922
DOI: 10.1021/jacsau.3c00696

Experimental method

X-RAY DIFFRACTION (2.3 Å)