5O84
Glutathione S-transferase Tau 23 (partially oxidized)
Summary for 5O84
Entry DOI | 10.2210/pdb5o84/pdb |
Related | 6EP6 6EP7 |
Descriptor | Glutathione S-transferase U23, FORMIC ACID, 1,2-ETHANEDIOL, ... (7 entities in total) |
Functional Keywords | glutathione s-transferase, tau, transferase |
Biological source | Arabidopsis thaliana (Mouse-ear cress) |
Cellular location | Cytoplasm, cytosol : Q9M9F1 |
Total number of polymer chains | 1 |
Total formula weight | 25802.77 |
Authors | Young, D.R.,Van Molle, I.,Tossounian, M.,Messens, J. (deposition date: 2017-06-12, release date: 2017-10-25, Last modification date: 2024-01-17) |
Primary citation | Tossounian, M.A.,Van Molle, I.,Wahni, K.,Jacques, S.,Gevaert, K.,Van Breusegem, F.,Vertommen, D.,Young, D.,Rosado, L.A.,Messens, J. Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage. Biochim. Biophys. Acta, 1862:775-789, 2018 Cited by PubMed Abstract: Glutathione transferases play an important role as detoxifying enzymes. In A. thaliana, elevated levels of reactive oxygen species (ROS), provoked during biotic and abiotic stress, influence the activity of GSTU23. The aim of this study is to determine the impact of oxidative stress on the function and structure of GSTU23. PubMed: 29031766DOI: 10.1016/j.bbagen.2017.10.007 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.88 Å) |
Structure validation
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