Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae

Proteins: Structure, Function and Genetics

Volumn 68, Issue 4, 2007, Pages 972-979

  Yu, Jiang ^a   Zhou, Cong Zhao ^a,b  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^b UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

Author keywords

Crystal structure; Glutathione reductase; Glutathionylation; Glycosylation; Saccharomyces cerevisiae

Indexed keywords

GLUTATHIONE DISULFIDE; GLUTATHIONE REDUCTASE; GLUTATHIONE REDUCTASE 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME STRUCTURE; ESCHERICHIA COLI; GLYCOSYLATION; MICROENVIRONMENT; PRIORITY JOURNAL; PROTEIN EXPRESSION; SACCHAROMYCES CEREVISIAE; STRUCTURE ANALYSIS;

BINDING SITES; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; CYTOPLASM; GLUTATHIONE; GLUTATHIONE REDUCTASE; INDICATORS AND REAGENTS; KINETICS; MITOCHONDRIA; MODELS, MOLECULAR; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

ESCHERICHIA COLI; HOMO SAPIENS; PICHIA PASTORIS; SACCHAROMYCES CEREVISIAE;

EID: 34548717039     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21354     Document Type: Article

References (41)

1. Jamieson DJ. Oxidative stress responses of the yeast Saccharomyces cerevisiae. Yeast 1998;14:1511-1527.
2. Carmel-Harel O, Storz G. Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu Rev Microbiol 2000;54:439-461.
3. Wheeler GL, Grant CM. Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae. Physiol Plant 2004;120:12-20.
4. Grant CM. Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions. Mol Microbiol 2001;39:533-541.
5. Chakravarthi S, Jessop CE, Bulleid NJ. The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress. EMBO Rep 2006;7:271-275.
6. Bass R, Ruddock LW, Klappa P, Freedman RB. A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. J Biol Chem 2004;279:5257-5262.
7. Hurd TR, Costa NJ, Dahm CC, Beer SM, Brown SE, Filipovska A, Murphy MP. Glutathionylation of mitochondrial proteins. Antioxid Redox Signal 2005;7:999-1010.
8. Sanchez G, Pedrozo Z, Domenech RJ, Hidalgo C, Donoso P. Tachycardia increases NADPH oxidase activity and RyR2 S-glutathionylation in ventricular muscle. J Mol Cell Cardiol 2005;39:982-991.
9. Casagrande S, Bonetto V, Fratelli M, Gianazza E, Eberini I, Massignan T, Salmona M, Chang G, Holmgren A, Ghezzi P. Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems. Proc Natl Acad Sci USA 2002;99:9745-9749.
10. Fratelli M, Demol H, Puype M, Casagrande S, Villa P, Eberini I, Vandekerckhove J, Gianazza E, Ghezzi P. Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells. Proteomics 2003;3:1154-1161.
11. Fratelli M, Demol H, Puype M, Casagrande S, Eberini I, Salmona M, Bonetto V, Mengozzi M, Duffieux F, Miclet E, Bachi A, Vandekerckhove J, Gianazza E, Ghezzi P. Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc Natl Acad Sci USA 2002;99:3505-3510.
12. Chrestensen CA, Starke DW, Mieyal JJ. Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis. J Biol Chem 2000;275:26556-26565.
13. Cross JV, Templeton DJ. Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain. Biochem J 2004;381:675-683.
14. Dalle-Donne J, Giustarini D, Rossi R, Colombo R, Milzani A. Reversible S-glutathionylation of Cys 374 regulates actin filament formation by inducing structural changes in the actin molecule. Free Radic Biol Med 2003;34:23-32.
15. Humphries KM, Juliano C, Taylor SS. Regulation of cAMP-dependent protein kinase activity by glutathionylation. J Biol Chem 2002;277:43505-43511.
16. Bohme CC, Arscott LD, Becker K, Schirmer RH, Williams CH Jr., Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme. J Biol Chem 2000;275:37317-37323.
17. Arscott LD, Gromer S, Schirmer RH, Becker K, Williams CH Jr., The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli. Proc Natl Acad Sci USA 1997;94:3621-3626.
18. Dalle-Donne I, Rossi R, Giustarini D, Colombo R, Milzani A. Actin S-glutathionylation: evidence against a thiol-disulphide exchange mechanism. Free Radic Biol Med 2003;35:1185-1193.
19. Hwang C, Sinskey AJ, Lodish HF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 1992;257:1496-1502
20. Outten CE, Culotta VC. Alternative start sites in the Saccharomyces cerevisiae GLR1 gene are responsible for mitochondrial and cytosolic isoforms of glutathione reductase. J Biol Chem 2004;279:7785-7791.
21. Mittl PR, Schulz GE. Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes. Protein Sci 1994;3:799-809.
22. Savvides SN, Karplus PA. Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. J Biol Chem 1996;271:8101-8107.
23. Leslie AGW.Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4/ESF-EACMB Newsletter on Protein Crystallography, No. 26, 1992.
24. Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 1994; 50: 760-767.
25. Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 1998;54:905-921.
26. Jones TA, Zou JY, Cowan SW, Kjeldgaard . Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
27. Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997;53:240-255.
28. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993;26:283-291.
29. DeLano WL. The PyMOL molecular graphics system. San Carlos, CA: DeLano Scientific; 2002.
30. Mavis RD, Stellwagen E. Purification and subunit structure of glutathione reductase from bakers' yeast. J Biol Chem 1968;243:809-814.
31. Schulz GE. Binding of nucleotides by proteins. Curr Opin Struct Biol 1992;2:61-67.
32. Schulz GE. Gene duplication in glutathione reductase. J Mol Biol 1980;138:335-347.
33. Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 1988;16:10881-10890.
34. Gouet P, Robert X, Courcelle E. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res 2003;31:3320-3323.
35. Pai EF, Schulz GE. The catalytic mechanism of glutathione reductase as derived from X-ray diffraction analyses of reaction intermediates. J Biol Chem 1983;258:1752-1757.
36. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
37. Michelet L, Zaffagnini M, Marchand C, Collin V, Decottignies P, Tsan P, Lancelin JM, Trost P, Miginiac-Maslow M, Noctor G, Lemaire SD. Glutathionylation of chloroplast thioredoxin f is a redox signaling mechanism in plants. Proc Natl Acad Sci USA 2005;102:16478-16483.
38. Lyles MM, Gilbert HF. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 1991;30:613-619.
39. Hayano T, Inaka K, Otsu M, Taniyama Y, Miki K, Matsushima M, Kikuchi M. PDI and glutathione-mediated reduction of the glutathionylated variant of human lysozyme. FEBS Lett 1993;328:203-208.
40. Grinna LS, Tschopp JF Size distribution and general structural features of N-linked oligosaccharides from the methylotrophic yeast, Pichia pastoris. Yeast 1989;5:107-115.
41. Massey V, Williams CH Jr., On the reaction mechanism of yeast glutathione reductase. J Biol Chem 1965;240:4470-4480.