5GXU
Cystal structure of Arabidopsis ATR2
Summary for 5GXU
| Entry DOI | 10.2210/pdb5gxu/pdb |
| Descriptor | NADPH--cytochrome P450 reductase 2, FLAVIN MONONUCLEOTIDE, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | nadph-cytochrome p450 reductase, oxidoreductase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Cellular location | Endoplasmic reticulum membrane ; Single-pass membrane protein ; Cytoplasmic side : Q9SUM3 |
| Total number of polymer chains | 2 |
| Total formula weight | 145132.35 |
| Authors | |
| Primary citation | Niu, G.,Zhao, S.,Wang, L.,Dong, W.,Liu, L.,He, Y. Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function FEBS J., 284:754-765, 2017 Cited by PubMed Abstract: Members of the cytochrome P450 family catalyze a variety of mono-oxygenase reactions, and for the eukaryotic membrane-bound members, NADPH is typically used as the reducing agent. The flavoprotein NADPH-cytochrome P450 reductase (CPR) enables electron transfer from NADPH to cytochrome P450 via its flavin cofactors. ATR2 is one of the two authentic CPR genes in the genome of the model plant Arabidopsis thaliana, and its product has been physiologically and kinetically characterized. Here, we report the 2.3 Å structure of Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) and find that the position of the two flavin cofactors differs from that of other known CPR structures. Mutation of residues related to possible interflavin electron transfer retains the reductase activity of ATR2, which suggests a direct electron transfer pathway between the flavins. In contrast, mutation of a single residue (R708) mediating interdomain interaction abolishes this activity. Because this residue is only conserved in plant CPRs, we speculate a plant-specific working mechanism as observed in ATR2. PubMed: 28103421DOI: 10.1111/febs.14017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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