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Oxidoreductase PDB id
1gra
Jmol
Contents
Protein chain
461 a.a. *
Ligands
FAD
NDP
GSH-GSH
Waters ×530
* Residue conservation analysis
PDB id:
1gra
Name: Oxidoreductase
Title: Substrate binding and catalysis by glutathione reductase as from refined enzyme: substrate crystal structures at 2 angs resolution
Structure: Glutathione reductase. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
Biol. unit: Dimer (from PQS)
Resolution:
2.00Å     R-factor:   0.157    
Authors: P.A.Karplus,G.E.Schulz
Key ref: P.A.Karplus and G.E.Schulz (1989). Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution. J Mol Biol, 210, 163-180. PubMed id: 2585516 DOI: 10.1016/0022-2836(89)90298-2
Date:
15-Dec-92     Release date:   31-Jan-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00390  (GSHR_HUMAN) -  Glutathione reductase, mitochondrial
Seq:
Struc: 		 
Seq:
Struc: 		522 a.a.
461 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.8.1.7  - Glutathione-disulfide reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 glutathione + NADP+ = glutathione disulfide + NADPH
2 × glutathione
Bound ligand (Het Group name = GSH)
corresponds exactly 		+ NADP(+)
 = glutathione disulfide
 + NADPH
      Cofactor: FAD
FAD
Bound ligand (Het Group name = FAD) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     soluble fraction   5 terms 
  Biological process     oxidation-reduction process   6 terms 
  Biochemical function     electron carrier activity     8 terms  

 

 
    reference    
 
 
DOI no: 10.1016/0022-2836(89)90298-2 J Mol Biol 210:163-180 (1989)
PubMed id: 2585516  
 
 
Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution.
P.A.Karplus, G.E.Schulz.
 
  ABSTRACT  
 
The X-ray structure analyses of four glutathione reductase complexes and derivatives have been extended to 2 A resolution and refined. The results are discussed in conjunction with the structure of the oxidized native enzyme known at 1.54 A resolution. While the residual co-ordinate errors are around 0.2 A, some significant shifts even in this range could be established. Points of particular interest are the 3.2 A approach of C4N of nicotinamide to N5F of flavin in hydride transfer geometry, the hydrogen bond geometries of the 2'-phosphate of NADPH as compared to inferior geometries for an inorganic phosphate binding together with NADH, the differential mobilities of parts of the substrates as derived from refined atomic temperature factors, and the stabilization of the thiolate of the proximal Cys63 by conformational changes of neighboring residues as well as by flavin. In addition, catalytically competent His467' is seen to interact more optimally with the sulfur of glutathione-I than with the distal sulfur of Cys58. The observed participation of water molecules for both NADPH and glutathione binding is so extensive that a prediction of the binding mode merely from the polypeptide structure would be very difficult. The accurately known geometries allowed us to draw some conclusions on the enzyme mechanism and suggest a possible scenario of the catalysis.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21321730 K.P.Bhabak, B.J.Bhuyan, and G.Mugesh (2011).
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  Dalton Trans, 40, 2099-2111.  
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  Antioxid Redox Signal, 13, 1231-1246.  
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  J Mol Biol, 390, 924-938.
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  Structure, 17, 713-724.  
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  Biochemistry, 47, 8080-8093.
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  J Mol Biol, 382, 371-384.
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  Proteins, 72, 936-945.
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  FEBS J, 275, 1350-1366.  
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  Annu Rev Plant Biol, 59, 143-166.  
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  Biochemistry, 46, 819-827.  
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  Protein Sci, 6, 2084-2096.  
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Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum.
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Catalysis by entropic guidance from enzymes.
  Biochemistry, 35, 15129-15133.  
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Negative electrostatic surface potential of protein sites specific for anionic ligands.
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The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.
  Structure, 4, 1413-1428.
PDB code: 1ofg
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PDB codes: 1dru 1drv 1drw
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Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor.
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PDB code: 1xan
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PDB code: 1aog
8789194 C.S.Poornima, and P.M.Dean (1995).
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  J Comput Aided Mol Des, 9, 521-531.  
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Trypanothione reductase from Leishmania donovani. Purification, characterisation and inhibition by trivalent antimonials.
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Chemical modification of the N-10 ribityl side chain of flavins. Effects on properties of flavoprotein disulfide oxidoreductases.
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The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state.
  Proteins, 18, 161-173.
PDB code: 1nda
  7881908 K.M.Fox, and P.A.Karplus (1994).
Old yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins.
  Structure, 2, 1089-1105.
PDB codes: 1oya 1oyb 1oyc
  7922042 M.J.Adams, G.H.Ellis, S.Gover, C.E.Naylor, and C.Phillips (1994).
Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism.
  Structure, 2, 651-668.
PDB codes: 1pgn 1pgo 1pgp 1pgq
8168518 M.L.Cunningham, M.J.Zvelebil, and A.H.Fairlamb (1994).
Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenicals.
  Eur J Biochem, 221, 285-295.  
  7833810 P.R.Mittl, A.Berry, N.S.Scrutton, R.N.Perham, and G.E.Schulz (1994).
Anatomy of an engineered NAD-binding site.
  Protein Sci, 3, 1504-1514.
PDB codes: 1ges 1get 1geu
  8061609 P.R.Mittl, and G.E.Schulz (1994).
Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes.
  Protein Sci, 3, 799-809.
PDB code: 1ger
  8298460 C.C.Correll, M.L.Ludwig, C.M.Bruns, and P.A.Karplus (1993).
Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin.
  Protein Sci, 2, 2112-2133.  
8477734 S.Bailey, K.Smith, A.H.Fairlamb, and W.N.Hunter (1993).
Substrate interactions between trypanothione reductase and N1-glutathionylspermidine disulphide at 0.28-nm resolution.
  Eur J Biochem, 213, 67-75.
PDB code: 1typ
8425532 T.Stehle, A.Claiborne, and G.E.Schulz (1993).
NADH binding site and catalysis of NADH peroxidase.
  Eur J Biochem, 211, 221-226.
PDB code: 2npx
1325638 A.Mattevi, G.Obmolova, J.R.Sokatch, C.Betzel, and W.G.Hol (1992).
The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 A resolution.
  Proteins, 13, 336-351.
PDB code: 1lvl
1584202 J.Peinado, J.Florindo, and J.López-Barea (1992).
Glutathione reductase from Saccharomyces cerevisiae undergoes redox interconversion in situ and in vivo.
  Mol Cell Biochem, 110, 135-143.  
1631094 K.I.Varughese, M.M.Skinner, J.M.Whiteley, D.A.Matthews, and N.H.Xuong (1992).
Crystal structure of rat liver dihydropteridine reductase.
  Proc Natl Acad Sci U S A, 89, 6080-6084.
PDB code: 1dhr
1453951 T.Aboagye-Kwarteng, K.Smith, and A.H.Fairlamb (1992).
Molecular characterization of the trypanothione reductase gene from Crithidia fasciculata and Trypanosoma brucei: comparison with other flavoprotein disulphide oxidoreductases with respect to substrate specificity and catalytic mechanism.
  Mol Microbiol, 6, 3089-3099.  
1957352 C.Walsh, M.Bradley, and K.Nadeau (1991).
Molecular studies on trypanothione reductase, a target for antiparasitic drugs.
  Trends Biochem Sci, 16, 305-309.  
1924336 J.Kuriyan, X.P.Kong, T.S.Krishna, R.M.Sweet, N.J.Murgolo, H.Field, A.Cerami, and G.B.Henderson (1991).
X-ray structure of trypanothione reductase from Crithidia fasciculata at 2.4-A resolution.
  Proc Natl Acad Sci U S A, 88, 8764-8768.
PDB code: 2tpr
2006135 U.Ermler, and G.E.Schulz (1991).
The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0 A resolution.
  Proteins, 9, 174-179.  
2065668 U.Ermler, S.Ghisla, V.Massey, and G.E.Schulz (1991).
Structural, spectroscopic and catalytic activity studies on glutathione reductase reconstituted with FAD analogues.
  Eur J Biochem, 199, 133-138.  
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