Catalytic features and crystal structure of a tau class glutathione transferase from Glycine max specifically upregulated in response to soybean mosaic virus infections

摘要: The plant tau class glutathione transferases (GSTs) play important roles in biotic and abiotic stress tolerance crops weeds. In this study, we systematically examined the catalytic structural features of a GST isoenzyme from Glycine max (GmGSTU10-10). GmGSTU10-10 is unique soybean that specifically expressed response to caused by mosaic virus (SMV) infections. was cloned, Escherichia coli, purified characterized. results showed catalyzes several different reactions exhibits wide substrate specificity. Of particular importance finding enzyme shows high antioxidant function acts as hydroperoxidase. addition, its Km for GSH significantly lower, compared other GSTs, suggesting able perform efficient catalysis under conditions where concentration reduced low (e.g. oxidative stress). crystal structure solved molecular replacement at 1.6A resolution complex with sulfenic acid (GSOH). Structural analysis shares same overall fold domain organization cytosolic GSTs; however, major variations were identified helix H9 upper part H4 affect size active site pockets, recognition mechanism. present study provide new information into diversity give further insights regulation enzymatic functions gene superfamily.