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Identification of Key Residues Associated with the Interaction between Plutella xylostella Sigma-Class Glutathione S‑Transferase and the Inhibitor S‑Hexyl Glutathione

作者:   来源:科研办   发布日期:2018-10-08  浏览次数:

       论文信息:Jiyuan Liu, Yifan Li, Zhen Tian, Hong Sun, Xi’en Chen, Shengli Zheng, Yalin Zhang. J. Agric. Food Chem. 2018, 66, 10169−10178.

       JCR分区Q1,中科院大类一区,IF=3.412

       论文摘要:Glutathione S-transferases (GSTs) are important detoxification enzymes involved in the development of metabolic resistance in Plutella xylostella. Uncovering the interactions between representative PxGSTs and the inhibitor S-hexyl glutathione (GTX), helps in the development of effective PxGST inhibitors for resistance management. As the PxGST mostseverely inhibited by GTX, PxGSTσ (sigma-class PxGST) adopts the canonical fold of insect GSTs. The formation of the PxGSTσ−GTX complex is mainly driven by H-bond and hydrophobic interactions derived from the side chains of favorable residues. Of the residues composing the active site of PxGSTσ, Lys43 and Arg99 are two hot spots, first reported in the binding of GSH derivatives to GSTs. Such differences indicate the metabolism discrimination of different insect GSTs. Unfavorable interactions between the PxGSTσ active site and GTX are depicted as well. The research guides the discovery and optimization of PxGSTσ inhibitors.

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