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EMBO J. 1984 Jul; 3(7): 1443–1449.
PMCID: PMC557542

Conformational and functional similarities between glutaredoxin and thioredoxins.


The tertiary structures of thioredoxin from Escherichia coli and bacteriophage T4 have been compared and aligned giving a common fold of 68 C alpha atoms with a root mean square difference of 2.6 A. The amino acid sequence of glutaredoxin has been aligned to those of the thioredoxins assuming that glutaredoxin has the same common fold. A model of the glutaredoxin molecule was built on a vector display using this alignment and the T4 thioredoxin tertiary structure. By comparison of the model with those of the thioredoxins, we have identified a molecular surface area on one side of the redox-active S-S bridge which we suggest is the binding area of these molecules for redox interactions with other proteins. This area comprises residues 33-34, 75-76 and 91-93 in E. coli thioredoxin; 15-16, 65-66 and 76-78 in T4 thioredoxin and 12-13, 59-60 and 69-71 in glutaredoxin. In all three molecules, this part of the surface is flat and hydrophobic. Charged groups are completely absent. In contrast, there is a cluster of charged groups on the other side of the S-S bridge which we suggest participates in the mechanisms of the redox reactions. In particular, a lysine residue close to an aromatic ring is conserved in all molecules.

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Selected References

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  • Berglund O. Identification of a thioredoxin induced by bacteriophage T4. J Biol Chem. 1969 Nov 25;244(22):6306–6308. [PubMed]
  • Berglund O, Holmgren A. Thioredoxin reductase-mediated hydrogen transfer from Escherichia coli thioredoxin-(SH)2 to phage T4 thioredoxin-S2. J Biol Chem. 1975 Apr 25;250(8):2778–2782. [PubMed]
  • Hall DE, Baldesten A, Holmgren A, Reichard P. Yeast thioredoxin. Amino-acid sequence around the active-center disulfide of thioredoxin I and II. Eur J Biochem. 1971 Nov 11;23(2):328–335. [PubMed]
  • Holmgren A. Thioredoxin. 6. The amino acid sequence of the protein from escherichia coli B. Eur J Biochem. 1968 Dec 5;6(4):475–484. [PubMed]
  • Holmgren A. Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin. J Biol Chem. 1972 Apr 10;247(7):1992–1998. [PubMed]
  • Holmgren A. Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc Natl Acad Sci U S A. 1976 Jul;73(7):2275–2279. [PMC free article] [PubMed]
  • Holmgren A. Glutathione-dependent enzyme reactions of the phage T4 ribonucleotide reductase system. J Biol Chem. 1978 Oct 25;253(20):7424–7430. [PubMed]
  • Holmgren A. Glutathione-dependent synthesis of deoxyribonucleotides. Purification and characterization of glutaredoxin from Escherichia coli. J Biol Chem. 1979 May 10;254(9):3664–3671. [PubMed]
  • Holmgren A. Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action. J Biol Chem. 1979 Sep 25;254(18):9113–9119. [PubMed]
  • Holmgren A. Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem. 1979 Oct 10;254(19):9627–9632. [PubMed]
  • Holmgren A, Roberts G. Nuclear magnetic resonance studies of redox-induced conformational changes in thioredoxin from Escherichia coli. FEBS Lett. 1976 Dec 1;71(2):261–265. [PubMed]
  • Holmgren A, Söderberg BO, Eklund H, Brändén CI. Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2305–2309. [PMC free article] [PubMed]
  • Holmgren A, Ohlsson I, Grankvist ML. Thiroedoxin from Escherichia coli. Radioimmunological and enzymatic determinations in wild type cells and mutants defective in phage T7 DNA replication. J Biol Chem. 1978 Jan 25;253(2):430–436. [PubMed]
  • Holmgren A, Kallis GB, Nordström B. A mutant thioredoxin from Escherichia coli tsnC 7007 that is nonfunctional as subunit of phage T7 DNA polymerase. J Biol Chem. 1981 Mar 25;256(6):3118–3124. [PubMed]
  • Hög JO, Jörnvall H, Holmgren A, Carlquist M, Persson M. The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol. Eur J Biochem. 1983 Oct 17;136(1):223–232. [PubMed]
  • Ladenstein R, Epp O, Bartels K, Jones A, Huber R, Wendel A. Structure analysis and molecular model of the selenoenzyme glutathione peroxidase at 2.8 A resolution. J Mol Biol. 1979 Oct 25;134(2):199–218. [PubMed]
  • Mark DF, Richardson CC. Escherichia coli thioredoxin: a subunit of bacteriophage T7 DNA polymerase. Proc Natl Acad Sci U S A. 1976 Mar;73(3):780–784. [PMC free article] [PubMed]
  • Meng M, Hogenkamp HP. Purification, characterization, and amino acid sequence of thioredoxin from Corynebacterium nephridii. J Biol Chem. 1981 Sep 10;256(17):9174–9182. [PubMed]
  • Ohlsson I, Nordström B, Brändén CI. Structural and functional similarities within the coenzyme binding domains of dehydrogenases. J Mol Biol. 1974 Oct 25;89(2):339–354. [PubMed]
  • Sjöberg BM, Holmgren A. Studies on the structure of T4 thioredoxin. II. Amino acid sequence of the protein and comparison with thioredoxin from Escherichia coli. J Biol Chem. 1972 Dec 25;247(24):8063–8068. [PubMed]
  • Slabý I, Holmgren A. Structure and enzymatic functions of thioredoxin refolded by complementation of two tryptic peptide fragments. Biochemistry. 1979 Dec 11;18(25):5584–5591. [PubMed]
  • Stryer L, Holmgren A, Reichard P. Thioredoxin. A localized conformational change accompanying reduction of the protein to the sulfhydryl form. Biochemistry. 1967 Apr;6(4):1016–1020. [PubMed]
  • Söderberg BO, Sjöberg BM, Sonnerstam U, Brändén CI. Three-dimensional structure of thioredoxin induced by bacteriophage T4. Proc Natl Acad Sci U S A. 1978 Dec;75(12):5827–5830. [PMC free article] [PubMed]
  • Thelander L. Reaction mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Oxidation-reduction-active disulfides in the B1 subunit. J Biol Chem. 1974 Aug 10;249(15):4858–4862. [PubMed]
  • Thelander L, Reichard P. Reduction of ribonucleotides. Annu Rev Biochem. 1979;48:133–158. [PubMed]
  • Tsugita A, Maeda K, Schürmann P. Spinach chloroplast thioredoxins in evolutionary drift. Biochem Biophys Res Commun. 1983 Aug 30;115(1):1–7. [PubMed]

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