TY - JOUR
T1 - Structural characterization of the catalytic site of a Nilaparvata lugens delta-class glutathione transferase
AU - Yamamoto, Kohji
AU - Higashiura, Akifumi
AU - Hossain, Md Tofazzal
AU - Yamada, Naotaka
AU - Shiotsuki, Takahiro
AU - Nakagawa, Atsushi
N1 - Funding Information:
This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan , and a Research Grant for Young Investigators of Faculty of Agriculture, Kyushu University . This work was performed under the auspices of the Cooperative Research Program of Institute for Protein Research, Osaka University. The synchrotron radiation experiments were carried out at the BL44XU of SPring-8 with the approval of the Japan Synchrotron Radiation Research Institute (JASRI) (Proposal Nos. 2013A6862 and 2013B6862).
Publisher Copyright:
© 2014 Elsevier Inc.
PY - 2015/1/15
Y1 - 2015/1/15
N2 - Glutathione transferases (GSTs) are a major class of detoxification enzymes that play a central role in the defense against environmental toxicants and oxidative stress. Here, we studied the crystal structure of a delta-class glutathione transferase from Nilaparvata lugens, nlGSTD, to gain insights into its catalytic mechanism. The structure of nlGSTD in complex with glutathione, determined at a resolution of 1.7 Å, revealed that it exists as a dimer and its secondary and tertiary structures are similar to those of other delta-class GSTs. Analysis of a complex between nlGSTD and glutathione showed that the bound glutathione was localized to the glutathione-binding site. Site-directed mutagenesis of nlGSTD mutants indicated that amino acid residues Ser11, His52, Glu66, and Phe119 contribute to catalytic activity.
AB - Glutathione transferases (GSTs) are a major class of detoxification enzymes that play a central role in the defense against environmental toxicants and oxidative stress. Here, we studied the crystal structure of a delta-class glutathione transferase from Nilaparvata lugens, nlGSTD, to gain insights into its catalytic mechanism. The structure of nlGSTD in complex with glutathione, determined at a resolution of 1.7 Å, revealed that it exists as a dimer and its secondary and tertiary structures are similar to those of other delta-class GSTs. Analysis of a complex between nlGSTD and glutathione showed that the bound glutathione was localized to the glutathione-binding site. Site-directed mutagenesis of nlGSTD mutants indicated that amino acid residues Ser11, His52, Glu66, and Phe119 contribute to catalytic activity.
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U2 - 10.1016/j.abb.2014.12.001
DO - 10.1016/j.abb.2014.12.001
M3 - Article
C2 - 25497345
AN - SCOPUS:84919897648
SN - 0003-9861
VL - 566
SP - 36
EP - 42
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
ER -