Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5H5L

Structure of prostaglandin synthase D of Nilaparvata lugens

Summary for 5H5L
Entry DOI10.2210/pdb5h5l/pdb
DescriptorGlutathione s-transferase S2, GLUTATHIONE, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
Functional Keywordsglutathione, lepidoptera, prostaglandin, prostaglandin synthase, transferase
Biological sourceNilaparvata lugens (Brown planthopper)
Total number of polymer chains2
Total formula weight48066.88
Authors
Yamamoto, K.,Higashiura, A.,Suzuki, S.,Nakagawa, A. (deposition date: 2016-11-07, release date: 2017-09-20, Last modification date: 2023-11-08)
Primary citationYamamoto, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.999 Å)
Structure validation

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon