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Volumn 6, Issue 2, 1997, Pages 383-390

Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form

Author keywords

glutaredoxin; nuclear magnetic resonance; secondary structure; sequence specific assignments

Indexed keywords

GLUTAREDOXIN; NITROGEN 15; UNCLASSIFIED DRUG; CARBON; NITROGEN; OXIDOREDUCTASE; PROTEIN; PROTON; RECOMBINANT PROTEIN;

EID: 0030614688     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060214     Document Type: Article
Times cited : (12)

References (63)
  • 1
    • 0026664431 scopus 로고
    • Glutaredoxin homolog encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities
    • Ahn BY, Moss B. 1992. Glutaredoxin homolog encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities. Proc Natl Acad Sci USA 89:7060-7064.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7060-7064
    • Ahn, B.Y.1    Moss, B.2
  • 3
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules
    • Bartels C, Xia T, Billeter M, Güntert P, Wüthrich K. 1995. The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules. J Biomol NMR 6:1-10.
    • (1995) J Biomol NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 4
    • 0010285919 scopus 로고
    • Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy
    • Bax A, Subramanian S. 1986. Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy. J Magn Reson 67:565-569.
    • (1986) J Magn Reson , vol.67 , pp. 565-569
    • Bax, A.1    Subramanian, S.2
  • 6
    • 84985653913 scopus 로고
    • 1H-NMR titration shifts for studies of polypeptide conformation
    • 1H-NMR titration shifts for studies of polypeptide conformation. Biopolymers 18:299-311.
    • (1979) Biopolymers , vol.18 , pp. 299-311
    • Bündi, A.1    Wüthrich, K.2
  • 7
    • 0028181442 scopus 로고
    • The NMR solution structure of the mixed disulfide between E. coli glutaredoxin (C14S) and glutathione
    • Bushweller JH, Billeter M, Holmgren A, Wüthrich K. 1994. The NMR solution structure of the mixed disulfide between E. coli glutaredoxin (C14S) and glutathione. J Mol Biol 235:1585-1597.
    • (1994) J Mol Biol , vol.235 , pp. 1585-1597
    • Bushweller, J.H.1    Billeter, M.2    Holmgren, A.3    Wüthrich, K.4
  • 9
    • 0025261972 scopus 로고
    • Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy
    • Dyson HJ, Gippert GP, Case DA, Holmgren A, Wright PE. 1990. Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy. Biochemistry 29:4129-4136.
    • (1990) Biochemistry , vol.29 , pp. 4129-4136
    • Dyson, H.J.1    Gippert, G.P.2    Case, D.A.3    Holmgren, A.4    Wright, P.E.5
  • 11
    • 0025909444 scopus 로고
    • High-resolution three-dimensional structure of reduced recombinant thioredoxin in solution
    • Forman-Kay JD, Clore GM, Wingfield PT, Gronenborn AM. 1991. High-resolution three-dimensional structure of reduced recombinant thioredoxin in solution. Biochemistry 30:2685-2698.
    • (1991) Biochemistry , vol.30 , pp. 2685-2698
    • Forman-Kay, J.D.1    Clore, G.M.2    Wingfield, P.T.3    Gronenborn, A.M.4
  • 13
    • 0023654910 scopus 로고
    • The primary structure of pig liver thioltransferase
    • Gan ZR, Wells WW. 1987a. The primary structure of pig liver thioltransferase. J Biol Chem 262:6699-6703.
    • (1987) J Biol Chem , vol.262 , pp. 6699-6703
    • Gan, Z.R.1    Wells, W.W.2
  • 14
    • 0023654889 scopus 로고
    • Identification and reactivity of the catalytic site of pig liver thioltransferase
    • Gan ZR, Wells WW. 1987b. Identification and reactivity of the catalytic site of pig liver thioltransferase. J Biol Chem 262:6704-6797.
    • (1987) J Biol Chem , vol.262 , pp. 6704-6797
    • Gan, Z.R.1    Wells, W.W.2
  • 15
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • Gravina SA, Mieyal JJ. 1993. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry 32:3368-3376.
    • (1993) Biochemistry , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 17
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
    • Grzesiek S, Bax A. 1992. Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein. J Magn Reson 96:432-440.
    • (1992) J Magn Reson , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 18
    • 0026426079 scopus 로고
    • A common pattern between the TGF-β family and glutaredoxin
    • Guigó R, Smith TF. 1991. A common pattern between the TGF-β family and glutaredoxin. Biochem J 280:833-834.
    • (1991) Biochem J , vol.280 , pp. 833-834
    • Guigó, R.1    Smith, T.F.2
  • 19
    • 0000088628 scopus 로고
    • Processing of multi-dimensional NMR data with the new software PROSA
    • Güntert P, Dötsch V, Wider G, Wüthrich K. 1992. Processing of multi-dimensional NMR data with the new software PROSA. J Biomol NMR 2:619-629.
    • (1992) J Biomol NMR , vol.2 , pp. 619-629
    • Güntert, P.1    Dötsch, V.2    Wider, G.3    Wüthrich, K.4
  • 20
    • 2042476756 scopus 로고
    • Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione
    • Holmgren A. 1976. Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc Natl Acad Sci USA 73:2275-2279.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 2275-2279
    • Holmgren, A.1
  • 21
    • 0018786584 scopus 로고
    • Glutathione-dependent synthesis of deoxyribonucleotides. Purification and characterization of glutaredoxin from Escherichia coli
    • Holmgren A. 1979a. Glutathione-dependent synthesis of deoxyribonucleotides. Purification and characterization of glutaredoxin from Escherichia coli. J Biol Chem 254:3664-3671.
    • (1979) J Biol Chem , vol.254 , pp. 3664-3671
    • Holmgren, A.1
  • 22
    • 0018728098 scopus 로고
    • Reduction of disulfides by thioredoxin Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action
    • Holmgren A. 1979b. Reduction of disulfides by thioredoxin Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action. J Biol Chem 254:9113-9119.
    • (1979) J Biol Chem , vol.254 , pp. 9113-9119
    • Holmgren, A.1
  • 24
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. 1989. Thioredoxin and glutaredoxin systems. J Biol Chem 264: 13963-13966.
    • (1989) J Biol Chem , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 26
    • 0024326913 scopus 로고
    • Glutaredoxin from rabbit bone marrow. Purification, characterization and amino acid sequence determination by tandem mass spectrometry
    • Hopper S, Johnson RS, Biemann K. 1989. Glutaredoxin from rabbit bone marrow. Purification, characterization and amino acid sequence determination by tandem mass spectrometry. J Biol Chem 264:20438-20447.
    • (1989) J Biol Chem , vol.264 , pp. 20438-20447
    • Hopper, S.1    Johnson, R.S.2    Biemann, K.3
  • 27
    • 0026225733 scopus 로고
    • 13C-labeled protein using constant-time evolution
    • 13C-labeled protein using constant-time evolution. J Biomol NMR 1:299-304.
    • (1991) J Biomol NMR , vol.1 , pp. 299-304
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 28
    • 0029159834 scopus 로고
    • The structure of a reduced mutant T4 glutaredoxin
    • Ingelman M, Nordlund P, Eklund H. 1995. The structure of a reduced mutant T4 glutaredoxin. FEBS Lett 370:209-211.
    • (1995) FEBS Lett , vol.370 , pp. 209-211
    • Ingelman, M.1    Nordlund, P.2    Eklund, H.3
  • 31
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution
    • Katti SK, LeMaster DM, Eklund H. 1990. Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J Mol Biol 212:167-184.
    • (1990) J Mol Biol , vol.212 , pp. 167-184
    • Katti, S.K.1    LeMaster, D.M.2    Eklund, H.3
  • 32
    • 0028892388 scopus 로고
    • Crystal structure of thioltransferase at 2.2 Å resolution
    • Katti SK, Robbins AH, Yang Y, Wells WW. 1995. Crystal structure of thioltransferase at 2.2 Å resolution. Protein Sci 4:1998-2005.
    • (1995) Protein Sci , vol.4 , pp. 1998-2005
    • Katti, S.K.1    Robbins, A.H.2    Yang, Y.3    Wells, W.W.4
  • 33
    • 0008262893 scopus 로고
    • 1H-detected heteronuclear multiple-quantum correlation spectra
    • 1H-detected heteronuclear multiple-quantum correlation spectra. J Magn Reson 84:598-603.
    • (1989) J Magn Reson , vol.84 , pp. 598-603
    • Kay, L.E.1    Bax, A.2
  • 36
    • 0021753907 scopus 로고
    • The primary structure of calf thymus glutaredoxin. Homology with the corresponding Escherichia coli protein but elongation at both ends with an additional half-cysteine/cysteine pair
    • Klintrot IM, Höög JO, Jörnvall H, Holmgren A, Luthman M. 1984. The primary structure of calf thymus glutaredoxin. Homology with the corresponding Escherichia coli protein but elongation at both ends with an additional half-cysteine/cysteine pair. Eur J Biochem 144:417-423.
    • (1984) Eur J Biochem , vol.144 , pp. 417-423
    • Klintrot, I.M.1    Höög, J.O.2    Jörnvall, H.3    Holmgren, A.4    Luthman, M.5
  • 39
    • 0018470912 scopus 로고
    • Glutathione-dependent hydrogen donor system for calf thymus ribonucleoside diphosphate reductase
    • Luthman M, Eriksson S, Holmgren A, Thelander L. 1979. Glutathione-dependent hydrogen donor system for calf thymus ribonucleoside diphosphate reductase. Proc Natl Acad Sci USA 76:2158-2162.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 2158-2162
    • Luthman, M.1    Eriksson, S.2    Holmgren, A.3    Thelander, L.4
  • 40
    • 0020490790 scopus 로고
    • Glutaredoxin from calf thymus. I. Purification to homogeneity
    • Luthman M, Holmgren A. 1982. Glutaredoxin from calf thymus. I. Purification to homogeneity. J Biol Chem 257:6686-6690.
    • (1982) J Biol Chem , vol.257 , pp. 6686-6690
    • Luthman, M.1    Holmgren, A.2
  • 41
    • 0025887464 scopus 로고
    • Thioltransferase in human red blood cells: Kinetics and equilibrium
    • Mieyal JJ, Starke DW, Gravina SA, Hocevar BA. 1991. Thioltransferase in human red blood cells: Kinetics and equilibrium. Biochemistry 30:8883-8891.
    • (1991) Biochemistry , vol.30 , pp. 8883-8891
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Hocevar, B.A.4
  • 44
    • 0001689741 scopus 로고
    • Gradient enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram DR, Kay LE. 1994. Gradient enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J Magn Reson B 103:203-216.
    • (1994) J Magn Reson B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 45
    • 33845373878 scopus 로고
    • Multi-quantum-filtered two-dimensional correlated NMR spectroscopy of proteins
    • Muller N, Ernst RR, Wüthrich K. 1986. Multi-quantum-filtered two-dimensional correlated NMR spectroscopy of proteins. J Am Chem Soc 108:6482-6492.
    • (1986) J Am Chem Soc , vol.108 , pp. 6482-6492
    • Muller, N.1    Ernst, R.R.2    Wüthrich, K.3
  • 46
    • 45449123834 scopus 로고
    • Efficient purging scheme for proton-detected heteronuclear two-dimensional NMR
    • Otting G, Wüthrich K. 1988. Efficient purging scheme for proton-detected heteronuclear two-dimensional NMR. J Magn Reson 76:569-574.
    • (1988) J Magn Reson , vol.76 , pp. 569-574
    • Otting, G.1    Wüthrich, K.2
  • 47
    • 0028804668 scopus 로고
    • Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin
    • Padilla CA, Martìnez-Galisteo E, Bárcena JA, Spyrou G, Holmgren A. 1995. Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin. Eur J Biochem 227:27-34.
    • (1995) Eur J Biochem , vol.227 , pp. 27-34
    • Padilla, C.A.1    Martìnez-Galisteo, E.2    Bárcena, J.A.3    Spyrou, G.4    Holmgren, A.5
  • 48
    • 0030058359 scopus 로고    scopus 로고
    • High-level expression of fully active human glutaredoxin (thioltransferase) in E. coli and characterization of Cys 7 to Ser mutant protein
    • Padilla CA, Spyrou G, Holmgren A. 1996. High-level expression of fully active human glutaredoxin (thioltransferase) in E. coli and characterization of Cys 7 to Ser mutant protein. FEBS Lett 378:69-13
    • (1996) FEBS Lett , vol.378 , pp. 69-113
    • Padilla, C.A.1    Spyrou, G.2    Holmgren, A.3
  • 50
    • 0028773644 scopus 로고
    • The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin
    • Qin J, Clore GM, Gronenbom AM. 1994. The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure 2:503-522.
    • (1994) Structure , vol.2 , pp. 503-522
    • Qin, J.1    Clore, G.M.2    Gronenbom, A.M.3
  • 52
    • 0003840108 scopus 로고    scopus 로고
    • Department of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands
    • Rullmann JAC. 1996. AQUA, computer program. Department of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands.
    • (1996) AQUA, Computer Program
    • Rullmann, J.A.C.1
  • 54
    • 0347610773 scopus 로고
    • 13C nuclear magnetic resonance chemical shifts
    • 13C nuclear magnetic resonance chemical shifts. J Am Chem Soc 113:5490-5492.
    • (1991) J Am Chem Soc , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 56
    • 0025082330 scopus 로고
    • Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity
    • Wells WW, Xu DP, Yang YF, Rocque PA. 1990. Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. J Biol Chem 265:15361-15364.
    • (1990) J Biol Chem , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Xu, D.P.2    Yang, Y.F.3    Rocque, P.A.4
  • 58
    • 43949167657 scopus 로고
    • HNCACB. A high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins
    • Wittekind M, Mueller L. 1993. HNCACB. a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. J Magn Reson B 101:201-205.
    • (1993) J Magn Reson B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 60
    • 0027050496 scopus 로고
    • NMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteins
    • Xia T, Bushweller JH, Sodano P, Billeter M, Björnberg O, Holmgren A, Wüthrich K. 1992. NMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteins. Protein Sci 1:310-321.
    • (1992) Protein Sci , vol.1 , pp. 310-321
    • Xia, T.1    Bushweller, J.H.2    Sodano, P.3    Billeter, M.4    Björnberg, O.5    Holmgren, A.6    Wüthrich, K.7
  • 62
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced sensitivity pulsed field gradient NMR techniques. J Biomol NMR 4:845-858.
    • (1994) J Biomol NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 63
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiolsdisulfides in metabolic regulation
    • Ziegler DM. 1985. Role of reversible oxidation-reduction of enzyme thiolsdisulfides in metabolic regulation. Annu Rev Biochem 54:305-329.
    • (1985) Annu Rev Biochem , vol.54 , pp. 305-329
    • Ziegler, D.M.1


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