6QUQ
Crystal structure of glutathionylated glycolytic glyceraldehyde-3- phosphate dehydrogenase from Arabidopsis thaliana (AtGAPC1)
Summary for 6QUQ
| Entry DOI | 10.2210/pdb6quq/pdb |
| Related | 4Z0H |
| Descriptor | Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | rossman fold, oxidoreductase activity, nad, cytosolic, glutathione, oxidoreductase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 75649.35 |
| Authors | Fermani, S.,Zaffagnini, M.,Falini, G.,Trost, P. (deposition date: 2019-02-28, release date: 2019-12-04, Last modification date: 2024-01-24) |
| Primary citation | Zaffagnini, M.,Marchand, C.H.,Malferrari, M.,Murail, S.,Bonacchi, S.,Genovese, D.,Montalti, M.,Venturoli, G.,Falini, G.,Baaden, M.,Lemaire, S.D.,Fermani, S.,Trost, P. Glutathionylation primes soluble glyceraldehyde-3-phosphate dehydrogenase for late collapse into insoluble aggregates. Proc.Natl.Acad.Sci.USA, 116:26057-26065, 2019 Cited by PubMed Abstract: Protein aggregation is a complex physiological process, primarily determined by stress-related factors revealing the hidden aggregation propensity of proteins that otherwise are fully soluble. Here we report a mechanism by which glycolytic glyceraldehyde-3-phosphate dehydrogenase of (AtGAPC1) is primed to form insoluble aggregates by the glutathionylation of its catalytic cysteine (Cys149). Following a lag phase, glutathionylated AtGAPC1 initiates a self-aggregation process resulting in the formation of branched chains of globular particles made of partially misfolded and totally inactive proteins. GSH molecules within AtGAPC1 active sites are suggested to provide the initial destabilizing signal. The following removal of glutathione by the formation of an intramolecular disulfide bond between Cys149 and Cys153 reinforces the aggregation process. Physiological reductases, thioredoxins and glutaredoxins, could not dissolve AtGAPC1 aggregates but could efficiently contrast their growth. Besides acting as a protective mechanism against overoxidation, S-glutathionylation of AtGAPC1 triggers an unexpected aggregation pathway with completely different and still unexplored physiological implications. PubMed: 31772010DOI: 10.1073/pnas.1914484116 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.993 Å) |
Structure validation
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