Structural highlights
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Function
[OPR3_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 PubMed
X-ray crystallography typically uses a single set of coordinates and B factors to describe macromolecular conformations. Refinement of multiple copies of the entire structure has been previously used in specific cases as an alternative means of representing structural flexibility. Here, we systematically validate this method by using simulated diffraction data, and we find that ensemble refinement produces better representations of the distributions of atomic positions in the simulated structures than single-conformer refinements. Comparison of principal components calculated from the refined ensembles and simulations shows that concerted motions are captured locally, but that correlations dissipate over long distances. Ensemble refinement is also used on 50 experimental structures of varying resolution and leads to decreases in R(free) values, implying that improvements in the representation of flexibility observed for the simulated structures may apply to real structures. These gains are essentially independent of resolution or data-to-parameter ratio, suggesting that even structures at moderate resolution can benefit from ensemble refinement.
Ensemble refinement of protein crystal structures: validation and application.,Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr Structure. 2007 Sep;15(9):1040-52. PMID:17850744[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stintzi A, Browse J. The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis. Proc Natl Acad Sci U S A. 2000 Sep 12;97(19):10625-30. PMID:10973494 doi:http://dx.doi.org/10.1073/pnas.190264497
- ↑ Beynon ER, Symons ZC, Jackson RG, Lorenz A, Rylott EL, Bruce NC. The role of oxophytodienoate reductases in the detoxification of the explosive 2,4,6-trinitrotoluene by Arabidopsis. Plant Physiol. 2009 Sep;151(1):253-61. doi: 10.1104/pp.109.141598. Epub 2009 Jul , 15. PMID:19605548 doi:http://dx.doi.org/10.1104/pp.109.141598
- ↑ Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr. Ensemble refinement of protein crystal structures: validation and application. Structure. 2007 Sep;15(9):1040-52. PMID:17850744 doi:http://dx.doi.org/10.1016/j.str.2007.06.019
