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PDBsum entry 2grs
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Oxidoreductase (flavoenzyme) PDB id
2grs

 

 

 

 

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Contents
Protein chain
461 a.a.
Ligands
FAD
Superseded by: 3grs 3grs
PDB id:
2grs
Name: Oxidoreductase (flavoenzyme)
Structure: Glutathione reductase
Source: Human (homo sapiens) erythrocyte
Authors: G.E.Schulz,R.H.Schirmer
Key ref:
R.Thieme et al. (1981). Three-dimensional structure of glutathione reductase at 2 A resolution. J Mol Biol, 152, 763-782. PubMed id: 7334521 DOI: 10.1016/0022-2836(81)90126-1
Date:
23-Nov-81     Release date:   03-Feb-82    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 461 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1016/0022-2836(81)90126-1 J Mol Biol 152:763-782 (1981)
PubMed id: 7334521  
 
 
Three-dimensional structure of glutathione reductase at 2 A resolution.
R.Thieme, E.F.Pai, R.H.Schirmer, G.E.Schulz.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 3.
FIG. 3. Stereo vies of the chain fold of one complete subunit of glutathione reductase and of the chain folds of separate domains. The lines represen virtual bonds between consecutive C, atoms. All parts of the Figure correspond to the same orientation of the molecule. The numbers denote the sequence positions of first and last residue in the depicted chain. The molecular 2-fold axis is inserted with a dot as reference point. The N-terminal segment of residues 1 to 18 is omitted because it has no defined conformation. (a) Chain fold of one subunit containing FAD. (b) FAD-domain toether with the bound FAD. The ong rotrusion consisting of 2 a-helices reaches the molecular 2-fold axis at Cys90, which is marked by a dot. Cys90 forms a disulfide bridge with its counterpart in the other subunit. Cys58 		Figure 6.
FIG. 6. Strand arrangements in the 5 p-pleated sheets of glutathioe reductase. The amino acid esidues are given in one-letter code. The nmbers of the first and the last residue in each strand are nserted. The strand connections in the antiprallel parts of the sheets are given as dotted lines. Domain orders in sheets A and B are indicted by vertical broken lines. (A) Sheet shared by the FAD-and the entral-domain. The /l-structure of the antiprallel part is rather distorted. (B) j3-Meander of the FAD- domain with an additional parallel strand from the central-domain that is less well-ordered. (C) Parallel heet of the NADPH-domain. (D) P-Meander of the NADPH-domain with an additional parallel strand. (E) Antiparallel p-sheet of the interface-domain, The B-stranded part of this sheet is flat. In conrast, all other sheets shown here are twisted in the usal way; right-haded when viewed along the strands.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1981, 152, 763-782) copyright 1981.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18548475 G.Casi, G.Roelfes, and D.Hilvert (2008).
Selenoglutaredoxin as a glutathione peroxidase mimic.
  Chembiochem, 9, 1623-1631.  
18981569 M.Sentürk, I.Gülçin, M.Ciftci, and O.I.Küfrevioğlu (2008).
Dantrolene inhibits human erythrocyte glutathione reductase.
  Biol Pharm Bull, 31, 2036-2039.  
15922018 S.K.Krueger, and D.E.Williams (2005).
Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism.
  Pharmacol Ther, 106, 357-387.  
15454452 P.A.van den Berg, A.van Hoek, and A.J.Visser (2004).
Evidence for a novel mechanism of time-resolved flavin fluorescence depolarization in glutathione reductase.
  Biophys J, 87, 2577-2586.  
12829275 T.Barkay, S.M.Miller, and A.O.Summers (2003).
Bacterial mercury resistance from atoms to ecosystems.
  FEMS Microbiol Rev, 27, 355-384.  
12011076 I.F.Sevrioukova, and T.L.Poulos (2002).
Putidaredoxin reductase, a new function for an old protein.
  J Biol Chem, 277, 25831-25839.  
11213487 J.Qin, Y.Yang, A.Velyvis, and A.Gronenborn (2000).
Molecular views of redox regulation: three-dimensional structures of redox regulatory proteins and protein complexes.
  Antioxid Redox Signal, 2, 827-840.  
9678494 N.S.Ningaraj, and M.K.Rao (1998).
Disulfiram augments oxidative stress in rat brain following bilateral carotid artery occlusion.
  J Biomed Sci, 5, 226-230.  
9545063 P.A.van den Berg, A.van Hoek, C.D.Walentas, R.N.Perham, and A.J.Visser (1998).
Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductase.
  Biophys J, 74, 2046-2058.  
9151953 A.Nordhoff, C.Tziatzios, J.A.van den Broek, M.K.Schott, H.R.Kalbitzer, K.Becker, D.Schubert, and R.H.Schirmer (1997).
Denaturation and reactivation of dimeric human glutathione reductase--an assay for folding inhibitors.
  Eur J Biochem, 245, 273-282.
PDB code: 1alg
  8880899 G.Van Driessche, M.Koh, Z.W.Chen, F.S.Mathews, T.E.Meyer, R.G.Bartsch, M.A.Cusanovich, and J.J.Van Beeumen (1996).
Covalent structure of the flavoprotein subunit of the flavocytochrome c: sulfide dehydrogenase from the purple phototrophic bacterium Chromatium vinosum.
  Protein Sci, 5, 1753-1764.  
8631352 R.L.Krauth-Siegel, J.G.Müller, F.Lottspeich, and R.H.Schirmer (1996).
Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria.
  Eur J Biochem, 235, 345-350.  
8626496 S.N.Savvides, and P.A.Karplus (1996).
Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor.
  J Biol Chem, 271, 8101-8107.
PDB code: 1xan
7797549 T.C.Liu, L.G.Korotchkina, S.L.Hyatt, N.N.Vettakkorumakankav, and M.S.Patel (1995).
Spectroscopic studies of the characterization of recombinant human dihydrolipoamide dehydrogenase and its site-directed mutants.
  J Biol Chem, 270, 15545-15550.  
8147842 N.S.Scrutton (1994).
alpha/beta barrel evolution and the modular assembly of enzymes: emerging trends in the flavin oxidase/dehydrogenase family.
  Bioessays, 16, 115-122.  
8451239 C.W.Müller, and G.E.Schulz (1993).
Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop.
  Proteins, 15, 42-49.
PDB codes: 1e4v 1e4y
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
1409563 J.E.Jentoft, M.Shoham, D.Hurst, and M.S.Patel (1992).
A structural model for human dihydrolipoamide dehydrogenase.
  Proteins, 14, 88.  
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.  
1849605 A.C.Perry, N.Ni Bhriain, N.L.Brown, and D.A.Rouch (1991).
Molecular characterization of the gor gene encoding glutathione reductase from Pseudomonas aeruginosa: determinants of substrate specificity among pyridine nucleotide-disulphide oxidoreductases.
  Mol Microbiol, 5, 163-171.  
  1902462 J.A.Palmer, K.Hatter, and J.R.Sokatch (1991).
Cloning and sequence analysis of the LPD-glc structural gene of Pseudomonas putida.
  J Bacteriol, 173, 3109-3116.  
1684937 J.Benen, W.van Berkel, Z.Zak, T.Visser, C.Veeger, and A.de Kok (1991).
Lipoamide dehydrogenase from Azotobacter vinelandii: site-directed mutagenesis of the His450-Glu455 diad. Spectral properties of wild type and mutated enzymes.
  Eur J Biochem, 202, 863-872.  
1707373 M.S.Weiss, A.Kreusch, E.Schiltz, U.Nestel, W.Welte, J.Weckesser, and G.E.Schulz (1991).
The structure of porin from Rhodobacter capsulatus at 1.8 A resolution.
  FEBS Lett, 280, 379-382.  
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.  
2269305 H.Lohrer, and R.L.Krauth-Siegel (1990).
Purification and characterization of lipoamide dehydrogenase from Trypanosoma cruzi.
  Eur J Biochem, 194, 863-869.  
2107323 M.S.Johnson, M.J.Sutcliffe, and T.L.Blundell (1990).
Molecular anatomy: phyletic relationships derived from three-dimensional structures of proteins.
  J Mol Evol, 30, 43-59.  
  2400586 N.Guinec, M.Pagano, V.Dalet-Fumeron, and R.Engler (1990).
"In vitro" digestion of intact bovine lens capsules by four human lysosomal cysteine-proteinases.
  Biol Chem Hoppe Seyler, 371, 239-254.  
2298204 T.Sejlitz, C.Wernstedt, A.Engström, and H.Y.Neujahr (1990).
Amino acid sequences around the pyridoxal-5'-phosphate-binding sites of phenol hydroxylase.
  Eur J Biochem, 187, 225-228.  
2917566 G.Burns, T.Brown, K.Hatter, and J.R.Sokatch (1989).
Sequence analysis of the lpdV gene for lipoamide dehydrogenase of branched-chain-oxoacid dehydrogenase of Pseudomonas putida.
  Eur J Biochem, 179, 61-69.  
2682654 J.H.Hurley, P.E.Thorsness, V.Ramalingam, N.H.Helmers, D.E.Koshland, and R.M.Stroud (1989).
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.
  Proc Natl Acad Sci U S A, 86, 8635-8639.
PDB code: 3icd
2912729 P.A.Karplus, E.F.Pai, and G.E.Schulz (1989).
A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution.
  Eur J Biochem, 178, 693-703.  
2660100 P.A.Rice, and T.A.Steitz (1989).
Ribosomal protein L7/L12 has a helix-turn-helix motif similar to that found in DNA-binding regulatory proteins.
  Nucleic Acids Res, 17, 3757-3762.  
2653819 S.Ghisla, and V.Massey (1989).
Mechanisms of flavoprotein-catalyzed reactions.
  Eur J Biochem, 181, 1.  
2483872 T.J.Thekkumkara, G.Pons, S.Mitroo, J.E.Jentoft, and M.S.Patel (1989).
Molecular biology of the human pyruvate dehydrogenase complex: structural aspects of the E2 and E3 components.
  Ann N Y Acad Sci, 573, 113-129.  
2832161 A.H.Westphal, and A.de Kok (1988).
Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular cloning, organization and sequence analysis of the gene.
  Eur J Biochem, 172, 299-305.  
3338461 P.A.Karplus, R.L.Krauth-Siegel, R.H.Schirmer, and G.E.Schulz (1988).
Inhibition of human glutathione reductase by the nitrosourea drugs 1,3-bis(2-chloroethyl)-1-nitrosourea and 1-(2-chloroethyl)-3-(2-hydroxyethyl)-1-nitrosourea. A crystallographic analysis.
  Eur J Biochem, 171, 193-198.
PDB code: 1grh
  3286606 S.T.Cole, K.Eiglmeier, S.Ahmed, N.Honore, L.Elmes, W.F.Anderson, and J.H.Weiner (1988).
Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12.
  J Bacteriol, 170, 2448-2456.  
3255373 T.Kikuchi, G.Némethy, and H.A.Scheraga (1988).
Prediction of the packing arrangement of strands in beta-sheets of globular proteins.
  J Protein Chem, 7, 473-490.  
3581436 M.A.Rosemeyer (1987).
The biochemistry of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase.
  Cell Biochem Funct, 5, 79-95.  
3037534 R.A.Laddaga, L.Chu, T.K.Misra, and S.Silver (1987).
Nucleotide sequence and expression of the mercurial-resistance operon from Staphylococcus aureus plasmid pI258.
  Proc Natl Acad Sci U S A, 84, 5106-5110.  
  2827958 T.J.Foster (1987).
The genetics and biochemistry of mercury resistance.
  Crit Rev Microbiol, 15, 117-140.  
2410917 I.A.Wilson, D.H.Haft, E.D.Getzoff, J.A.Tainer, R.A.Lerner, and S.Brenner (1985).
Identical short peptide sequences in unrelated proteins can have different conformations: a testing ground for theories of immune recognition.
  Proc Natl Acad Sci U S A, 82, 5255-5259.  
3856839 I.Fita, and M.G.Rossmann (1985).
The NADPH binding site on beef liver catalase.
  Proc Natl Acad Sci U S A, 82, 1604-1608.
PDB codes: 7cat 8cat
3896786 M.C.Pinto, A.M.Mata, and J.López-Barea (1985).
The redox interconversion mechanism of Saccharomyces cerevisiae glutathione reductase.
  Eur J Biochem, 151, 275-281.  
3987692 R.L.Krauth-Siegel, R.H.Schirmer, and S.Ghisla (1985).
FAD analogues as prosthetic groups of human glutathione reductase. Properties of the modified enzyme species and comparisons with the active site structure.
  Eur J Biochem, 148, 335-344.  
6697994 M.Bilzer, R.L.Krauth-Siegel, R.H.Schirmer, T.P.Akerboom, H.Sies, and G.E.Schulz (1984).
Interaction of a glutathione S-conjugate with glutathione reductase. Kinetic and X-ray crystallographic studies.
  Eur J Biochem, 138, 373-378.  
6090218 M.J.Sternberg, and W.R.Taylor (1984).
Modelling the ATP-binding site of oncogene products, the epidermal growth factor receptor and related proteins.
  FEBS Lett, 175, 387-392.  
6653783 B.W.Dijkstra, W.J.Weijer, and R.K.Wierenga (1983).
Polypeptide chains with similar amino acid sequences but a distinctly different conformation. Bovine and porcine phospholipase A2.
  FEBS Lett, 164, 25-27.  
6617648 C.M.Visser (1983).
Reaction mechanism of flavin-dependent hydroxylation. Evolution of a non-imitable enzyme.
  Eur J Biochem, 135, 543-548.  
6840083 G.Zanetti, V.Massey, and B.Curti (1983).
FAD analogues as mechanistic and 'binding-domain' probes of spinach ferredoxin-NADP+ reductase.
  Eur J Biochem, 132, 201-205.  
6861757 H.von Bahr-Lindström, Y.M.Galante, M.Persson, and H.Jörnvall (1983).
The primary structure of subunit II of NADH dehydrogenase from bovine-heart mitochondria.
  Eur J Biochem, 134, 145-150.  
6406227 W.J.Weijer, J.Hofsteenge, J.J.Beintema, R.K.Wierenga, and J.Drenth (1983).
p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 2. Fitting of the amino-acid sequence to the tertiary structure.
  Eur J Biochem, 133, 109-118.  
7140736 G.Zanetti, D.Cidaria, and B.Curti (1982).
Preparation of apoprotein from spinach ferredoxin-NADP+ reductase. Studies on the resolution process and characterization of the FAD reconstituted holoenzyme.
  Eur J Biochem, 126, 453-458.  
7060551 R.L.Krauth-Siegel, R.Blatterspiel, M.Saleh, E.Schiltz, R.H.Schirmer, and R.Untucht-Grau (1982).
Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain.
  Eur J Biochem, 121, 259-267.  
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 code is shown on the right.

 

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