4Z0H
X-ray structure of cytoplasmic glyceraldehyde-3-phosphate dehydrogenase (GapC1) complexed with NAD
Summary for 4Z0H
| Entry DOI | 10.2210/pdb4z0h/pdb |
| Related | 3K2B |
| Descriptor | Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | cytoplasm, glycolysis, rossmann fold, nad complex, oxidoreductase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Cellular location | Cytoplasm: P25858 |
| Total number of polymer chains | 2 |
| Total formula weight | 75034.71 |
| Authors | Fermani, S.,Zaffagnini, M.,Orru, R.,Falini, G.,Trost, P. (deposition date: 2015-03-26, release date: 2016-04-13, Last modification date: 2024-01-10) |
| Primary citation | Zaffagnini, M.,Fermani, S.,Calvaresi, M.,Orru, R.,Iommarini, L.,Sparla, F.,Falini, G.,Bottoni, A.,Trost, P. Tuning Cysteine Reactivity and Sulfenic Acid Stability by Protein Microenvironment in Glyceraldehyde-3-Phosphate Dehydrogenases of Arabidopsis thaliana. Antioxid. Redox Signal., 24:502-517, 2016 Cited by PubMed Abstract: Cysteines and H2O2 are fundamental players in redox signaling. Cysteine thiol deprotonation favors the reaction with H2O2 that generates sulfenic acids with dual electrophilic/nucleophilic nature. The protein microenvironment surrounding the target cysteine is believed to control whether sulfenic acid can be reversibly regulated by disulfide formation or irreversibly oxidized to sulfinates/sulfonates. In this study, we present experimental oxidation kinetics and a quantum mechanical/molecular mechanical (QM/MM) investigation to elucidate the reaction of H2O2 with glycolytic and photosynthetic glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana (cytoplasmic AtGAPC1 and chloroplastic AtGAPA, respectively). PubMed: 26650776DOI: 10.1089/ars.2015.6417 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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