Structural highlights
Publication Abstract from PubMed
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 1.7A, 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.
Structural characterization of the catalytic site of a Nilaparvata lugens delta-class glutathione transferase.,Yamamoto K, Higashiura A, Hossain MT, Yamada N, Shiotsuki T, Nakagawa A Arch Biochem Biophys. 2014 Dec 9;566C:36-42. doi: 10.1016/j.abb.2014.12.001. PMID:25497345[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yamamoto K, Higashiura A, Hossain MT, Yamada N, Shiotsuki T, Nakagawa A. Structural characterization of the catalytic site of a Nilaparvata lugens delta-class glutathione transferase. Arch Biochem Biophys. 2014 Dec 9;566C:36-42. doi: 10.1016/j.abb.2014.12.001. PMID:25497345 doi:http://dx.doi.org/10.1016/j.abb.2014.12.001
