TY - JOUR
T1 - Molecular structure of a prostaglandin D synthase requiring glutathione from the brown planthopper, Nilaparvata lugens
AU - Yamamoto, Kohji
AU - Higashiura, Akifumi
AU - Suzuki, Mamoru
AU - Aritake, Kosuke
AU - Urade, Yoshihiro
AU - Nakagawa, Atsushi
N1 - Funding Information:
This work was supported in part by a Grant-in-Aid for Scientific Research (KAKENHI, 15H04611) from MEXT, and by a Research Grant for Young Investigators of the Department of Agriculture, Kyushu University. This work was performed under the Cooperative Research Program of the Institute for Protein Research, Osaka University. The synchrotron radiation experiments were performed at the BL44XU of SPring-8 with the approval of the Japan Synchrotron Radiation Research Institute (JASRI) (Proposal No. 2015B6555, 2016A6654 and 2016B6654).
Publisher Copyright:
© 2017 Elsevier Inc.
PY - 2017/10/14
Y1 - 2017/10/14
N2 - 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 PGH2 to PGD2. 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.
AB - 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 PGH2 to PGD2. 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.
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U2 - 10.1016/j.bbrc.2017.08.032
DO - 10.1016/j.bbrc.2017.08.032
M3 - Article
C2 - 28803983
AN - SCOPUS:85027581588
SN - 0006-291X
VL - 492
SP - 166
EP - 171
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -