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PDBsum entry 2hsa

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
2hsa
Jmol
Contents
Protein chains
374 a.a. *
Ligands
SO4 ×2
FMN ×2
Metals
_CL
Waters ×503
* Residue conservation analysis
PDB id:
2hsa
Name: Oxidoreductase
Title: Crystal structure of 12-oxophytodienoate reductase 3 (opr3) from tomato
Structure: 12-oxophytodienoate reductase 3. Chain: b, a. Synonym: 12-oxophytodienoate-10,11-reductase 3, opda- reductase 3, leopr3. Engineered: yes
Source: Solanum lycopersicum. Organism_taxid: 4081. Gene: opr3. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
1.50Å     R-factor:   0.225     R-free:   0.255
Authors: C.Breithaupt,T.Clausen,R.Huber
Key ref:
C.Breithaupt et al. (2006). Crystal structure of 12-oxophytodienoate reductase 3 from tomato: self-inhibition by dimerization. Proc Natl Acad Sci U S A, 103, 14337-14342. PubMed id: 16983071 DOI: 10.1073/pnas.0606603103
Date:
21-Jul-06     Release date:   12-Sep-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9FEW9  (OPR3_SOLLC) -  12-oxophytodienoate reductase 3
Seq:
Struc:
396 a.a.
374 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.3.1.42  - 12-oxophytodienoate reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 8-((1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl)octanoate + NADP+ = (15Z)-12-oxophyto-10,15-dienoate + NADPH
8-((1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl)octanoate
+ NADP(+)
= (15Z)-12-oxophyto-10,15-dienoate
+ NADPH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     peroxisome   1 term 
  Biological process     oxidation-reduction process   18 terms 
  Biochemical function     catalytic activity     4 terms  

 

 
    reference    
 
 
DOI no: 10.1073/pnas.0606603103 Proc Natl Acad Sci U S A 103:14337-14342 (2006)
PubMed id: 16983071  
 
 
Crystal structure of 12-oxophytodienoate reductase 3 from tomato: self-inhibition by dimerization.
C.Breithaupt, R.Kurzbauer, H.Lilie, A.Schaller, J.Strassner, R.Huber, P.Macheroux, T.Clausen.
 
  ABSTRACT  
 
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.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. OPR3 catalyzes the reduction of 9S,13S-OPDA to 1S,2S-3-oxo- 2(2'[Z]-pentenyl)-cyclopentane-1-octanoate (OPC-8:0).
Figure 5.
Fig. 5. Central section of the dimer interface of protomer A (red; amino acids are marked with an asterisk) and protomer B (yellow) of OPR3. In the crystal structure, a sulfate ion mediates various intermolecular contacts. The position of the sulfate ion would fit very well with that of the phosphate group of a phosphorylated Tyr-364 (blue).
 
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20461254 C.Stueckler, N.J.Mueller, C.K.Winkler, S.M.Glueck, K.Gruber, G.Steinkellner, and K.Faber (2010).
Bioreduction of alpha-methylcinnamaldehyde derivatives: chemo-enzymatic asymmetric synthesis of Lilial and Helional.
  Dalton Trans, 39, 8472-8476.  
21270958 C.Stueckler, T.C.Reiter, N.Baudendistel, and K.Faber (2010).
Nicotinamide-independent asymmetric bioreduction of CC-bonds via disproportionation of enones catalyzed by enoate reductases.
  Tetrahedron, 66, 663-667.  
  20037473 G.Bonaventure, and I.T.Baldwin (2010).
New insights into the early biochemical activation of jasmonic acid biosynthesis in leaves.
  Plant Signal Behav, 5, 287-289.  
20704658 M.Stumpe, C.Göbel, B.Faltin, A.K.Beike, B.Hause, K.Himmelsbach, J.Bode, R.Kramell, C.Wasternack, W.Frank, R.Reski, and I.Feussner (2010).
The moss Physcomitrella patens contains cyclopentenones but no jasmonates: mutations in allene oxide cyclase lead to reduced fertility and altered sporophyte morphology.
  New Phytol, 188, 740-749.  
19695649 A.J.Koo, and G.A.Howe (2009).
The wound hormone jasmonate.
  Phytochemistry, 70, 1571-1580.  
19473329 A.J.Koo, X.Gao, A.D.Jones, and G.A.Howe (2009).
A rapid wound signal activates the systemic synthesis of bioactive jasmonates in Arabidopsis.
  Plant J, 59, 974-986.  
19166624 G.Steinkellner, R.Rader, G.G.Thallinger, C.Kratky, and K.Gruber (2009).
VASCo: computation and visualization of annotated protein surface contacts.
  BMC Bioinformatics, 10, 32.  
19025383 J.Browse (2009).
Jasmonate passes muster: a receptor and targets for the defense hormone.
  Annu Rev Plant Biol, 60, 183-205.  
19416520 W.Li, B.Liu, L.Yu, D.Feng, H.Wang, and J.Wang (2009).
Phylogenetic analysis, structural evolution and functional divergence of the 12-oxo-phytodienoate acid reductase gene family in plants.
  BMC Evol Biol, 9, 90.  
18780388 C.Wasternack, and I.Feussner (2008).
Multifunctional enzymes in oxylipin metabolism.
  Chembiochem, 9, 2373-2375.  
17938955 T.Tani, H.Sobajima, K.Okada, T.Chujo, S.Arimura, N.Tsutsumi, M.Nishimura, H.Seto, H.Nojiri, and H.Yamane (2008).
Identification of the OsOPR7 gene encoding 12-oxophytodienoate reductase involved in the biosynthesis of jasmonic acid in rice.
  Planta, 227, 517-526.  
17513307 C.Wasternack (2007).
Jasmonates: an update on biosynthesis, signal transduction and action in plant stress response, growth and development.
  Ann Bot (Lond), 100, 681-697.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.