5YRY
Crystal structure of C-terminal redox domain of APR1 from Arabidopsis thaliana
Summary for 5YRY
| Entry DOI | 10.2210/pdb5yry/pdb |
| Descriptor | 5'-adenylylsulfate reductase 1, chloroplastic (2 entities in total) |
| Functional Keywords | redox domain, sulfer assimilatory, aps reductase, oxidoreductase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 14132.12 |
| Authors | Hsu, C.H. (deposition date: 2017-11-11, release date: 2018-11-14, Last modification date: 2024-03-27) |
| Primary citation | Chen, F.F.,Chien, C.Y.,Cho, C.C.,Chang, Y.Y.,Hsu, C.H. C-terminal Redox Domain ofArabidopsisAPR1 is a Non-Canonical Thioredoxin Domain with Glutaredoxin Function. Antioxidants (Basel), 8:-, 2019 Cited by PubMed Abstract: Sulfur is an essential nutrient that can be converted into utilizable metabolic forms to produce sulfur-containing metabolites in plant. Adenosine 5'-phosphosulfate (APS) reductase (APR) plays a vital role in catalyzing the reduction of activated sulfate to sulfite, which requires glutathione. Previous studies have shown that the C-terminal domain of APR acts as a glutathione-dependent reductase. The crystal structure of the C-terminal redox domain of APR1 (AtAPR1) shows a conserved α/β thioredoxin fold, but not a glutaredoxin fold. Further biochemical studies of the redox domain from AtAPR1 provided evidence to support the structural observation. Collectively, our results provide structural and biochemical information to explain how the thioredoxin fold exerts the glutaredoxin function in APR. PubMed: 31597378DOI: 10.3390/antiox8100461 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.698 Å) |
Structure validation
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