5H5L

Structure of prostaglandin synthase D of Nilaparvata lugens

5H5L の概要

• エントリーDOI: 10.2210/pdb5h5l/pdb
• 分子名称: Glutathione s-transferase S2, GLUTATHIONE, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: glutathione, lepidoptera, prostaglandin, prostaglandin synthase, transferase
• 由来する生物種: Nilaparvata lugens (Brown planthopper)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48066.88

構造登録者

Yamamoto, K.,Higashiura, A.,Suzuki, S.,Nakagawa, A. (登録日: 2016-11-07, 公開日: 2017-09-20, 最終更新日: 2023-11-08)

主引用文献

Yamamoto, K.,Higashiura, A.,Suzuki, M.,Aritake, K.,Urade, Y.,Nakagawa, A.
Molecular structure of a prostaglandin D synthase requiring glutathione from the brown planthopper, Nilaparvata lugens
Biochem. Biophys. Res. Commun., 492:166-171, 2017

PubMed Abstract: Prostaglandins are involved in many physiological processes, and prostaglandin synthases facilitate the detoxification of xenobiotics as well as endogenous compounds, such as through glutathione conjugation. Specifically, prostaglandin D synthase (PGDS) catalyzes the isomerization of PGH to PGD. Here we report the identification and structural analysis of PGDS from the brown planthopper rice pest Nilaparvata lugens (nlPGDS), which belongs to the sigma-class glutathione transferases. The structure of nlPGDS in complex with glutathione was determined at a resolution of 2.0 Å by X-ray crystallography. Bound glutathione was localized to the glutathione-binding site (G-site). Enzyme activity measurements following site-directed mutagenesis of nlPGDS indicated that amino acid residues Tyr8, Leu14, Trp39, Lys43, Gln50, Val51, Gln63, and Ser64 in the G-site contribute to its catalytic activity. To our knowledge, this represents the first report of a PGDS in insects. Our findings provide insights into the mechanism of nlPGDS activity and potentially that of other insects and therefore may facilitate the development of more effective and safe insecticides.

PubMed: 28803983
DOI: 10.1016/j.bbrc.2017.08.032

実験手法

X-RAY DIFFRACTION (1.999 Å)