5LOL
Glutathione-bound Dehydroascorbate Reductase 2 of Arabidopsis thaliana
Summary for 5LOL
| Entry DOI | 10.2210/pdb5lol/pdb |
| Descriptor | Glutathione S-transferase DHAR2, GLUTATHIONE, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | dehydroascorbate reductase, glutathione dehydrogenase, transferase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Cellular location | Cytoplasm, cytosol : Q9FRL8 |
| Total number of polymer chains | 1 |
| Total formula weight | 24087.54 |
| Authors | Young, D.R.,Pallo, A.,Bodra, N.,Messens, J. (deposition date: 2016-08-09, release date: 2017-06-07, Last modification date: 2024-01-10) |
| Primary citation | Bodra, N.,Young, D.,Astolfi Rosado, L.,Pallo, A.,Wahni, K.,De Proft, F.,Huang, J.,Van Breusegem, F.,Messens, J. Arabidopsis thaliana dehydroascorbate reductase 2: Conformational flexibility during catalysis. Sci Rep, 7:42494-42494, 2017 Cited by PubMed Abstract: Dehydroascorbate reductase (DHAR) catalyzes the glutathione (GSH)-dependent reduction of dehydroascorbate and plays a direct role in regenerating ascorbic acid, an essential plant antioxidant vital for defense against oxidative stress. DHAR enzymes bear close structural homology to the glutathione transferase (GST) superfamily of enzymes and contain the same active site motif, but most GSTs do not exhibit DHAR activity. The presence of a cysteine at the active site is essential for the catalytic functioning of DHAR, as mutation of this cysteine abolishes the activity. Here we present the crystal structure of DHAR2 from Arabidopsis thaliana with GSH bound to the catalytic cysteine. This structure reveals localized conformational differences around the active site which distinguishes the GSH-bound DHAR2 structure from that of DHAR1. We also unraveled the enzymatic step in which DHAR releases oxidized glutathione (GSSG). To consolidate our structural and kinetic findings, we investigated potential conformational flexibility in DHAR2 by normal mode analysis and found that subdomain mobility could be linked to GSH binding or GSSG release. PubMed: 28195196DOI: 10.1038/srep42494 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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