Skip to main content
Log in

NMR solution structure of the reduced form of thioredoxin 2 from Saccharomyces cerevisiae

  • NMR Structue Note
  • Published:
Journal of Biomolecular NMR Aims and scope Submit manuscript

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3

Abbreviations

Trx:

thioredoxin

References

  • Bao R, Chen Y, Tang YJ, Janin J, Zhou CZ (2007) Crystal structure of the yeast cytoplasmic thioredoxin Trx2. Proteins 66:246–249

    Article  Google Scholar 

  • Bax A, Grzesiek S (1993) Methodological advances in protein NMR. Acc Chem Res 26:131–138

    Article  Google Scholar 

  • Brunger AT, Adams PD, Clore GM, Delano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges N, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Cryst D 54:905–921

    Article  Google Scholar 

  • Buchanan BB (1991) Regulation of CO2 assimilation in oxygenic photosynthesis—the ferredoxin thioredoxin system—Perspective on its discovery, present status, and future-development. Arch Biochem Biophys 288:1

    Article  Google Scholar 

  • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMR Pipe—a multidimensional spectral processing system based on unix pipes. J Biomol NMR 6:277–293

    Article  Google Scholar 

  • Doublie S, Tabor S, Long AM, Richardson CC, Ellenberger T (1998) Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 angstrom resolution. Nature 391:251–258

    Article  ADS  Google Scholar 

  • Fesik SW, Eaton HL, Olejniczak ET, Zuiderweg ERP, McIntosh LP, Dahlquist FW (1990) 2D and 3D NMR-spectroscopy employing C-13-C-13 magnetization transfer by isotropic mixing—Spin system-identification in large proteins. J Am Chem Soc 112:886–888

    Article  Google Scholar 

  • Forman-Kay JD, Clore GM, Wingfield PT, Gronenborn AM (1991) High-resolution 3-dimensional structure of reduced recombinant human thioredoxin in solution. Biochemistry (USA) 30:2685–2698

    Google Scholar 

  • Holm L, Sander C (1995) DALI - A network tool for protein-structure comparison. Trends Biochem Sci 20(11):478–480

    Article  Google Scholar 

  • Holmgren A (1985) Thioredoxin. Annu Rev Biochem 54:237–271

    Article  Google Scholar 

  • Jeng MF, Campbell AP, Begley T, Holmgren A, Case DA, Wright PE, Dyson HJ (1994) High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. Structure 2(9):853–868

    Article  Google Scholar 

  • Johnson BA, Blevins RA (1994) NMR View—a computer-program for the visualization and analysis of NMR data. J Biomol NMR 4:603–614

    Article  Google Scholar 

  • Kang SW, Chae HZ, Seo MS, Rhee SG (1998) Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J Biol Chem 273:6297–6302

    Article  Google Scholar 

  • Katti SK, Lemaster DM, Eklund H (1990) J Mol Biol 212(1):167–184

    Article  Google Scholar 

  • Koradi R, Billeter M, Wuthrich K (1996) Crystal-structure of thioredoxin from Escherichia coli at 1.68A resolution. J Mol Graph 14:51–55, 29–32

    Google Scholar 

  • Laskowski RA, Rullmann JAC, MacArthur MW, Kaptein R, Thornton JM (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8(4):477–486

    Article  Google Scholar 

  • Laurent TC, Moore EC, Reichard P (1964) Enzymatic synthesis of deoxyribonucleotides. Isolation + characterization of thioredoxin hydrogen donor from Escherichia coli B. J Biol Chem 239:3436–3444

    Google Scholar 

  • Menchise V, Corbier C, Didierjean C, Saviano M, Benedetti E, Jacquot JP, Aubry A (2001) Crystal structure of the wild-type and D30A mutant thioredoxin of Chlamydomonas reinhardtii and implications for the catalytic mechanism. Biochem J 359:65–75

    Article  Google Scholar 

  • Monje-Casas F, Michan C, Pueyo C (2004) Absolute transcript levels of thioredoxin- and glutathione-dependent redox systems in Saccharomyces cerevisiae: response to stress and modulation with growth. Biochem J 383:139–147

    Article  Google Scholar 

  • Montelione GT, Wagner G (1990) Conformation-independent sequential NMR connections in isotope-enriched polypeptides by H-1-C-13-N-15 triple-resonance experiments. J Magn Reson 87:183–188

    Google Scholar 

  • Perona JJ, Craik CS (1997) Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. J Biol Chem 272(48):29987–29990

    Article  Google Scholar 

  • Pinheiro AS, Amorim GC, Netto LE, Valente AP, Almeida FCL (2006) (1) H, (13) C and (15) N Resonance assignments for the reduced forms of thioredoxin 1 and 2 from S. cerevisiae. J Biomol NMR 36(5):35

    Article  Google Scholar 

  • Qin J, Clore GM, Gronenborn AM (1994) The high-resolution 3-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure 2:503–522

    Article  Google Scholar 

  • Qin J, Clore GM, Kennedy WM, Huth JR, Gronenborn AM (1995) Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF-kappa-B. Structure 3:289–297

    Article  Google Scholar 

  • Schenk H, Klein M, Erdbrugger W, Droge W, Schulze-Osthoff K (1994) Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-kappa-B and AP-1. Proc Natl Acad Sci USA 91:1672–1676

    Article  ADS  Google Scholar 

  • Valente AP, Miyamoto CA, Almeida FCL (2006) Implications of protein conformational diversity for binding and development of new biological active compounds. Curr Med Chem 13:3697–3703

    Article  Google Scholar 

  • Wahl MC, Irmler A, Hecker B, Schirmer RH, Becker K (2005) Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster. J Mol Biol 345:1119–1130

    Article  Google Scholar 

Download references

Acknowledgements

This work was supported by Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Programas de Núcleos de Excelência (CNPq/PRONEX), Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ) and Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES). We thank Dr. Catarina Akiko Miyamoto and Prof. Franklin Rumjanek for the english review.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Fabio C. L. Almeida.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Amorim, G.C., Pinheiro, A.S., Netto, L.E.S. et al. NMR solution structure of the reduced form of thioredoxin 2 from Saccharomyces cerevisiae . J Biomol NMR 38, 99–104 (2007). https://doi.org/10.1007/s10858-007-9144-z

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10858-007-9144-z

Keywords

Navigation