2g5w
From Proteopedia
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.
Structural highlights
FunctionOPR3_ARATH Specifically cleaves olefinic bonds in cyclic enones. Involved in the biosynthesis of jasmonic acid (JA) and perhaps in biosynthesis or metabolism of other oxylipin signaling moleclules. Required for the spatial and temporal regulation of JA levels during dehiscence of anthers, promoting the stomium degeneration program. In vitro, reduces 9S,13S-12-oxophytodienoic acid (9S,13S-OPDA) and 9R,13R-OPDA to 9S,13S-OPC-8:0 and 9R,13R-OPC-8:0, respectively. Can detoxify the explosive 2,4,6-trinitrotoluene (TNT) in vitro by catalyzing its nitroreduction to form hydroxylamino-dinitrotoluene (HADNT).[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed12-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 (9S,13S)-12-oxophytodienoate [(9S,13S)-OPDA]. However, there has been no structural information about the interaction between OPRs and the physiologically relevant (9S,13S)-OPDA. Here we report the crystal structure of Arabidopsis thaliana OPR3 in complex with 8-iso prostaglandin A1 (8-iso PGA(1)) which has the same stereochemistry in the cyclopentenone ring as in the physiologically relevant 9S,13S-OPDA. This structure reveals a new binding mode for substrate that likely contributes to the relaxed stereospecificity observed for AtOPR3. Crystal structure of Arabidopsis thaliana 12-oxophytodienoate reductase isoform 3 in complex with 8-iso prostaglandin A(1).,Han BW, Malone TE, Kim DJ, Bingman CA, Kim HJ, Fox BG, Phillips GN Jr Proteins. 2011 Nov;79(11):3236-41. doi: 10.1002/prot.23153. Epub 2011 Sep 13. PMID:21915915[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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