3WYW: Structural Characterization Of Catalytic Site Of A Nilaparvata Lugens Delta-class Glutathione Transferase

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.
PDB ID: 3WYWDownload
MMDB ID: 125954
PDB Deposition Date: 2014/9/9
Updated in MMDB: 2015/01
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 3WYW: dimeric; determined by author and by software (PISA)
Molecular Components in 3WYW
Label Count Molecule
Proteins (2 molecules)
Glutathione S-transferase
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

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