2hs8: Difference between revisions
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|PDB= 2hs8 |SIZE=350|CAPTION= <scene name='initialview01'>2hs8</scene>, resolution 1.9Å | |PDB= 2hs8 |SIZE=350|CAPTION= <scene name='initialview01'>2hs8</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene> | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/12-oxophytodienoate_reductase 12-oxophytodienoate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.42 1.3.1.42] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/12-oxophytodienoate_reductase 12-oxophytodienoate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.42 1.3.1.42] </span> | ||
|GENE= OPR3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4081 Solanum lycopersicum]) | |GENE= OPR3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4081 Solanum lycopersicum]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2hs6|2HS6]], [[2hsa|2HSA]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hs8 OCA], [http://www.ebi.ac.uk/pdbsum/2hs8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hs8 RCSB]</span> | |||
}} | }} | ||
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[[Category: Clausen, T.]] | [[Category: Clausen, T.]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: alpha beta 8 barrel]] | [[Category: alpha beta 8 barrel]] | ||
[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
[[Category: jasmonate biosynthesis]] | [[Category: jasmonate biosynthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:34:43 2008'' | ||
Revision as of 03:34, 31 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | OPR3 (Solanum lycopersicum) | ||||||
| Activity: | 12-oxophytodienoate reductase, with EC number 1.3.1.42 | ||||||
| Related: | 2HS6, 2HSA
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the Y364F mutant of 12-oxophytodienoate reductase 3 from tomato
OverviewOverview
12-Oxophytodienoate reductase (OPR) 3, a homologue of old yellow enzyme (OYE), catalyzes the reduction of 9S,13S-12-oxophytodienoate to the corresponding cyclopentanone, which is subsequently converted to the plant hormone jasmonic acid (JA). JA and JA derivatives, as well as 12-oxophytodienoate and related cyclopentenones, are known to regulate gene expression in plant development and defense. Together with other oxygenated fatty acid derivatives, they form the oxylipin signature in plants, which resembles the pool of prostaglandins in animals. Here, we report the crystal structure of OPR3 from tomato and of two OPR3 mutants. Although the catalytic residues of OPR3 and related OYEs are highly conserved, several characteristic differences can be discerned in the substrate-binding regions, explaining the remarkable substrate stereoselectivity of OPR isozymes. Interestingly, OPR3 crystallized as an extraordinary self-inhibited dimer. Mutagenesis studies and biochemical analysis confirmed a weak dimerization of OPR3 in vitro, which correlated with a loss of enzymatic activity. Based on structural data of OPR3, a putative mechanism for a strong and reversible dimerization of OPR3 in vivo that involves phosphorylation of OPR3 is suggested. This mechanism could contribute to the shaping of the oxylipin signature, which is critical for fine-tuning gene expression in plants.
About this StructureAbout this Structure
2HS8 is a Single protein structure of sequence from Solanum lycopersicum. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of 12-oxophytodienoate reductase 3 from tomato: self-inhibition by dimerization., Breithaupt C, Kurzbauer R, Lilie H, Schaller A, Strassner J, Huber R, Macheroux P, Clausen T, Proc Natl Acad Sci U S A. 2006 Sep 26;103(39):14337-42. Epub 2006 Sep 18. PMID:16983071
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