3WYW

Structural characterization of catalytic site of a Nilaparvata lugens delta-class glutathione transferase

Summary for 3WYW

• Entry DOI: 10.2210/pdb3wyw/pdb
• Descriptor: Glutathione S-transferase, GLUTATHIONE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: glutathione conjugation, glutathione, transferase
• Biological source: Nilaparvata lugens (Brown planthopper)
• Total number of polymer chains: 2
• Total formula weight: 48621.32

Authors

Yamamoto, K.,Higashiura, A.,Nakagawa, A. (deposition date: 2014-09-09, release date: 2015-01-14, Last modification date: 2024-03-20)

Primary citation

Yamamoto, K.,Higashiura, A.,Hossain, M.T.,Yamada, N.,Shiotsuki, T.,Nakagawa, A.
Structural characterization of the catalytic site of a Nilaparvata lugens delta-class glutathione transferase.
Arch.Biochem.Biophys., 566C:36-42, 2014

PubMed Abstract: 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 1.7Å, 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.

PubMed: 25497345
DOI: 10.1016/j.abb.2014.12.001

Experimental method

X-RAY DIFFRACTION (1.7 Å)