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PDBsum entry 1vji

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Plant protein PDB id
1vji

 

 

 

 

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Contents
Protein chain
351 a.a. *
Ligands
FMN
Waters ×107
* Residue conservation analysis
PDB id:
1vji
Name: Plant protein
Title: Gene product of at1g76680 from arabidopsis thaliana
Structure: 12-oxophytodienoate reductase (opr1). Chain: a. Engineered: yes
Source: Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: at1g76680. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.00Å     R-factor:   0.206     R-free:   0.293
Authors: G.E.Wesenberg,D.W.Smith,G.N.Phillips Jr.,K.A.Johnson,C.A.Bingman, Center For Eukaryotic Structural Genomics (Cesg)
Key ref:
B.G.Fox et al. (2005). X-ray structure of Arabidopsis At1g77680, 12-oxophytodienoate reductase isoform 1. Proteins, 61, 206-208. PubMed id: 16080145 DOI: 10.1002/prot.20533
Date:
24-Feb-04     Release date:   16-Mar-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q8LAH7  (OPR1_ARATH) -  12-oxophytodienoate reductase 1 from Arabidopsis thaliana
Seq:
Struc:
372 a.a.
351 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: (1S,2S)-OPC-8 + NADP+ = (9S,13S,15Z)-12-oxophyto-10,15-dienoate + NADPH + H+
(1S,2S)-OPC-8
+ NADP(+)
= (9S,13S,15Z)-12-oxophyto-10,15-dienoate
+ NADPH
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1002/prot.20533 Proteins 61:206-208 (2005)
PubMed id: 16080145  
 
 
X-ray structure of Arabidopsis At1g77680, 12-oxophytodienoate reductase isoform 1.
B.G.Fox, T.E.Malone, K.A.Johnson, S.E.Madson, D.Aceti, C.A.Bingman, P.G.Blommel, B.Buchan, B.Burns, J.Cao, C.Cornilescu, J.Doreleijers, J.Ellefson, R.Frederick, H.Geetha, D.Hruby, W.B.Jeon, T.Kimball, J.Kunert, J.L.Markley, C.Newman, A.Olson, F.C.Peterson, G.N.Phillips, J.Primm, B.Ramirez, N.S.Rosenberg, M.Runnels, K.Seder, J.Shaw, D.W.Smith, H.Sreenath, J.Song, M.R.Sussman, S.Thao, D.Troestler, E.Tyler, R.Tyler, E.Ulrich, D.Vinarov, F.Vojtik, B.F.Volkman, G.Wesenberg, R.L.Wrobel, J.Zhang, Q.Zhao, Z.Zolnai.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. A: Stereo representation of the X-ray structure of Arabidopsis OPR1 (1VJI) showing the position of FMN and the putative substrate-binding loop (violet). B: comparison of the positions of the putative substrate-binding loop of OPR1 (violet) with those observed in structures of Lycopersicon esculentum (tomato) OPR1 (grey) and Arabidopsis OPR3 (green). Positions obtained from alignment of the backbone atoms of each structure with Arabidopsis OPR1. The position of bound 9R,13R-OPDA in the 1ICQ structure is also shown (grey).The Arabidopsis OPR1 loop consists of P132-P149, the tomato OPR1 loop consists of residues G136-R153, and the Arabidopsis OPR3 loop consists of I133-Y150. In the tomato OPR1 loop, the backbone traces from 1ICQ (with 9R, 13R-OPDA bound) and 1ICS (with PEG bound) are indistinguishable.
 
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 61, 206-208) copyright 2005.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.  
16983071 C.Breithaupt, R.Kurzbauer, H.Lilie, A.Schaller, J.Strassner, R.Huber, P.Macheroux, and T.Clausen (2006).
Crystal structure of 12-oxophytodienoate reductase 3 from tomato: self-inhibition by dimerization.
  Proc Natl Acad Sci U S A, 103, 14337-14342.
PDB codes: 2hs6 2hs8 2hsa
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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