2G5W
X-ray crystal structure of Arabidopsis thaliana 12-oxophytodienoate reductase isoform 3 (AtOPR3) in complex with 8-iso prostaglandin A1 and its cofactor, flavin mononucleotide.
Summary for 2G5W
| Entry DOI | 10.2210/pdb2g5w/pdb |
| Related | 1Q45 |
| Descriptor | 12-oxophytodienoate reductase 3, FLAVIN MONONUCLEOTIDE, (8S,12S)-15S-HYDROXY-9-OXOPROSTA-10Z,13E-DIEN-1-OIC ACID, ... (4 entities in total) |
| Functional Keywords | at2g06050, opr isoform 3, flavoprotein, flavoenzyme, oxidoreductase, xenobiotic reductase, old yellow enzyme, secondary messenger, structural genomics functional follow-up study, protein structure initiative, psi, center for eukaryotic structural genomics, cesg |
| Biological source | Arabidopsis thaliana (thale cress) |
| Cellular location | Peroxisome : Q9FUP0 |
| Total number of polymer chains | 2 |
| Total formula weight | 87067.94 |
| Authors | Han, B.W.,Malone, T.E.,Bingman, C.A.,Wesenberg, G.E.,Phillips Jr., G.N.,Fox, B.G.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2006-02-23, release date: 2006-04-04, Last modification date: 2023-08-30) |
| Primary citation | Han, B.W.,Malone, T.E.,Kim, D.J.,Bingman, C.A.,Kim, H.J.,Fox, B.G.,Phillips, G.N. Crystal structure of Arabidopsis thaliana 12-oxophytodienoate reductase isoform 3 in complex with 8-iso prostaglandin A(1). Proteins, 79:3236-3241, 2011 Cited by PubMed Abstract: 12-Oxophytodienoate reductase 3 (OPR3), one of the enzymes involved in the biosynthesis of the plant hormone jasmonic acid (JA), catalyzes the reduction of the cyclopentenone ring of (9,13)-12-oxophytodienoate [(9,13)-OPDA]. However, there has been no structural information about the interaction between OPRs and the physiologically relevant (9,13)-OPDA. Here we report the crystal structure of OPR3 in complex with 8- prostaglandin A1 (8- PGA) which has the same stereochemistry in the cyclopentenone ring as in the physiologically relevant 9,13-OPDA. This structure reveals a new binding mode for substrate that likely contributes to the relaxed stereospecificity observed for AtOPR3. PubMed: 21915915DOI: 10.1002/prot.23153 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.576 Å) |
Structure validation
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