6F05
ARABIDOPSIS THALIANA GSTF9, GSO3 BOUND
Summary for 6F05
Entry DOI | 10.2210/pdb6f05/pdb |
Related | 6EZY 6F01 |
Descriptor | Glutathione S-transferase F9, GLUTATHIONE SULFONIC ACID, GLYCEROL, ... (5 entities in total) |
Functional Keywords | transferase, phi class, peroxidase, gso3 |
Biological source | Arabidopsis thaliana (Mouse-ear cress) |
Total number of polymer chains | 10 |
Total formula weight | 246019.32 |
Authors | Tossounian, M.A.,Wahni, K.,VanMolle, I.,Vertommen, D.,Rosado, L.,Messens, J. (deposition date: 2017-11-17, release date: 2018-08-15, Last modification date: 2024-01-17) |
Primary citation | Tossounian, M.A.,Wahni, K.,Van Molle, I.,Vertommen, D.,Astolfi Rosado, L.,Messens, J. Redox-regulated methionine oxidation of Arabidopsis thaliana glutathione transferase Phi9 induces H-site flexibility. Protein Sci., 28:56-67, 2019 Cited by PubMed Abstract: Glutathione transferase enzymes help plants to cope with biotic and abiotic stress. They mainly catalyze the conjugation of glutathione (GSH) onto xenobiotics, and some act as glutathione peroxidase. With X-ray crystallography, kinetics, and thermodynamics, we studied the impact of oxidation on Arabidopsis thaliana glutathione transferase Phi 9 (GSTF9). GSTF9 has no cysteine in its sequence, and it adopts a universal GST structural fold characterized by a typical conserved GSH-binding site (G-site) and a hydrophobic co-substrate-binding site (H-site). At elevated H O concentrations, methionine sulfur oxidation decreases its transferase activity. This oxidation increases the flexibility of the H-site loop, which is reflected in lower activities for hydrophobic substrates. Determination of the transition state thermodynamic parameters shows that upon oxidation an increased enthalpic penalty is counterbalanced by a more favorable entropic contribution. All in all, to guarantee functionality under oxidative stress conditions, GSTF9 employs a thermodynamic and structural compensatory mechanism and becomes substrate of methionine sulfoxide reductases, making it a redox-regulated enzyme. PubMed: 29732642DOI: 10.1002/pro.3440 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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