6EL3
Structure of Progesterone 5beta-Reductase from Arabidopsis thaliana in complex with NADP
Summary for 6EL3
| Entry DOI | 10.2210/pdb6el3/pdb |
| Descriptor | 3-oxo-Delta(4,5)-steroid 5-beta-reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, CHLORIDE ION, ... (9 entities in total) |
| Functional Keywords | short chain dehydrogenase/reductase (sdr) fold, homodimer, nadp binding site, oxidoreductase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
| Total number of polymer chains | 6 |
| Total formula weight | 268900.79 |
| Authors | Muller, Y.A.,Schmidt, K.,Egerer-Sieber, C. (deposition date: 2017-09-27, release date: 2018-09-05, Last modification date: 2024-01-17) |
| Primary citation | Schmidt, K.,Petersen, J.,Munkert, J.,Egerer-Sieber, C.,Hornig, M.,Muller, Y.A.,Kreis, W. PRISEs (progesterone 5 beta-reductase and/or iridoid synthase-like 1,4-enone reductases): Catalytic and substrate promiscuity allows for realization of multiple pathways in plant metabolism. Phytochemistry, 156:9-19, 2018 Cited by PubMed Abstract: PRISEs (progesterone 5β-reductase and/or iridoid synthase-like 1,4-enone reductases) are involved in cardenolide and iridoid biosynthesis. We here investigated a PRISE (rAtSt5βR) from Arabidopsis thaliana, a plant producing neither cardenolides nor iridoids. The structure of rAtSt5βR was elucidated with X-ray crystallography and compared to the known structures of PRISEs from Catharanthus roseus (rCrISY) and Digitalis lanata (rDlP5βR). The three enzymes show a high degree of sequence and structure conservation in the active site. Amino acids previously considered to allow discrimination between progesterone 5β-reductase and iridoid synthase were interchanged among rAtSt5βR, rCrISY and rDlP5βR applying site-directed mutagenesis. Structural homologous substitutions had different effects, and changes in progesterone 5β-reductase and iridoid synthase activity were not correlated in all cases. Our results help to explain fortuitous emergence of metabolic pathways and product accumulation. The fact that PRISEs are found ubiquitously in spermatophytes insinuates that PRISEs might have a more general function in plant metabolism such as, for example, the detoxification of reactive carbonyl species. PubMed: 30172078DOI: 10.1016/j.phytochem.2018.08.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.899 Å) |
Structure validation
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