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Volumn 23, Issue 8, 2004, Pages 1709-1719

Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD

Author keywords

Crystal structure; Disulfide exchange; DsbC; DsbD; Oxidative protein folding

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; DISULFIDE; DISULFIDE ISOMERASE; DSBA PROTEIN; ISOMERASE; PROTEIN DSBC; PROTEIN DSBD; THIOREDOXIN; UNCLASSIFIED DRUG;

EID: 2442607486     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600178     Document Type: Article
Times cited : (115)

References (58)
  • 1
    • 0030830073 scopus 로고    scopus 로고
    • A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins
    • Andersen CL, Matthey-Dupraz A, Missiakas D, Raina S (1997) A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins. Mol Microbiol 26:121-132
    • (1997) Mol Microbiol , vol.26 , pp. 121-132
    • Andersen, C.L.1    Matthey-Dupraz, A.2    Missiakas, D.3    Raina, S.4
  • 2
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • Bader M, Muse W, Ballou DP, Gassner C, Bardwell JC (1999) Oxidative protein folding is driven by the electron transport system. Cell 98: 217-227
    • (1999) Cell , vol.98 , pp. 217-227
    • Bader, M.1    Muse, W.2    Ballou, D.P.3    Gassner, C.4    Bardwell, J.C.5
  • 3
    • 0034714289 scopus 로고    scopus 로고
    • Disulfide bonds are generated by quinone reduction
    • Bader MW, Xie T, Yu CA, Bardwell JC (2000) Disulfide bonds are generated by quinone reduction. J Biol Chem 275: 26082-26088
    • (2000) J Biol Chem , vol.275 , pp. 26082-26088
    • Bader, M.W.1    Xie, T.2    Yu, C.A.3    Bardwell, J.C.4
  • 5
    • 0033583239 scopus 로고    scopus 로고
    • In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
    • Bessette PH, Cotto JJ, Gilbert HF, Georgiou G (1999) In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG. J Biol Chem 274: 7784-7792
    • (1999) J Biol Chem , vol.274 , pp. 7784-7792
    • Bessette, P.H.1    Cotto, J.J.2    Gilbert, H.F.3    Georgiou, G.4
  • 7
    • 0034011364 scopus 로고    scopus 로고
    • Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm
    • Chung J, Chen T, Missiakas D (2000) Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm. Mol Microbiol 35: 1099-1109
    • (2000) Mol Microbiol , vol.35 , pp. 1099-1109
    • Chung, J.1    Chen, T.2    Missiakas, D.3
  • 8
    • 0036224573 scopus 로고    scopus 로고
    • Oxidative protein folding in bacteria
    • Collet JF, Bardwell JC (2002) Oxidative protein folding in bacteria. Mol Microbiol 44:1-8
    • (2002) Mol Microbiol , vol.44 , pp. 1-8
    • Collet, J.F.1    Bardwell, J.C.2
  • 10
    • 0027446271 scopus 로고
    • Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli
    • Dailey FE, Berg HC (1993) Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli. Proc Natl Acad Sci USA 90:1043-1047
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1043-1047
    • Dailey, F.E.1    Berg, H.C.2
  • 11
    • 0028953741 scopus 로고
    • Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase
    • Darby NJ, Creighton TE (1995) Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase. Biochemistry 34: 3576-3587
    • (1995) Biochemistry , vol.34 , pp. 3576-3587
    • Darby, N.J.1    Creighton, T.E.2
  • 13
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82: 70-77
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 15
    • 0034099457 scopus 로고    scopus 로고
    • Escherichia coli DipZ: Anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function
    • Gordon EH, Page MD, Willis AC, Ferguson SJ (2000) Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function. Mol Microbiol 35: 1360-1374
    • (2000) Mol Microbiol , vol.35 , pp. 1360-1374
    • Gordon, E.H.1    Page, M.D.2    Willis, A.C.3    Ferguson, S.J.4
  • 16
    • 0037018912 scopus 로고    scopus 로고
    • Thiol-disulfide exchange in an immunoglobulin-like fold: Structure of the N-terminal domain of DsbD
    • Goulding CW, Sawaya MR, Parseghian A, Lim V, Eisenberg D, Missiakas D (2002) Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD. Biochemistry 41: 6920-6927
    • (2002) Biochemistry , vol.41 , pp. 6920-6927
    • Goulding, C.W.1    Sawaya, M.R.2    Parseghian, A.3    Lim, V.4    Eisenberg, D.5    Missiakas, D.6
  • 17
    • 0042815104 scopus 로고    scopus 로고
    • Mechanism of the electron transfer catalyst DsbB from Escherichia coli
    • Grauschopf U, Fritz A, Glockshuber R (2003) Mechanism of the electron transfer catalyst DsbB from Escherichia coli. EMBO J 22: 3503-3513
    • (2003) EMBO J , vol.22 , pp. 3503-3513
    • Grauschopf, U.1    Fritz, A.2    Glockshuber, R.3
  • 19
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18: 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 20
    • 0037119945 scopus 로고    scopus 로고
    • The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: Crystal structure of the DsbC-DsbDalpha complex
    • Haebel PW, Goldstone D, Katzen F, Beckwith J, Metcalf P (2002) The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex. EMBO J 21: 4774-4784
    • (2002) EMBO J , vol.21 , pp. 4774-4784
    • Haebel, P.W.1    Goldstone, D.2    Katzen, F.3    Beckwith, J.4    Metcalf, P.5
  • 21
    • 0033525640 scopus 로고    scopus 로고
    • Random circular permutation of DsbA reveals segments that are essential for protein folding and stability
    • Hennecke J, Sebbel P, Glockshuber R (1999) Random circular permutation of DsbA reveals segments that are essential for protein folding and stability. J Mol Biol 286: 1197-1215
    • (1999) J Mol Biol , vol.286 , pp. 1197-1215
    • Hennecke, J.1    Sebbel, P.2    Glockshuber, R.3
  • 22
    • 0037431958 scopus 로고    scopus 로고
    • Disulfide bond isomerization in prokaryotes
    • Hiniker A, Bardwell JC (2003) Disulfide bond isomerization in prokaryotes. Biochemistry 42: 1179-1185
    • (2003) Biochemistry , vol.42 , pp. 1179-1185
    • Hiniker, A.1    Bardwell, J.C.2
  • 24
    • 0031776171 scopus 로고    scopus 로고
    • A single dipeptide sequence modulates the redox properties of a whole enzyme family
    • Huber-Wunderlich M, Glockshuber R (1998) A single dipeptide sequence modulates the redox properties of a whole enzyme family. Fold Des 3: 161-171
    • (1998) Fold Des , vol.3 , pp. 161-171
    • Huber-Wunderlich, M.1    Glockshuber, R.2
  • 25
    • 0031297461 scopus 로고    scopus 로고
    • Specific versus non-specific contacts in protein crystals
    • Janin J (1997) Specific versus non-specific contacts in protein crystals. Nat Struct Biol 4: 973-974
    • (1997) Nat Struct Biol , vol.4 , pp. 973-974
    • Janin, J.1
  • 26
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S, Thornton JM (1996) Principles of protein-protein interactions. Proc Natl Acad Sci USA 93: 13-20
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 27
    • 0031565725 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites using patch analysis
    • Jones S, Thornton JM (1997) Prediction of protein-protein interaction sites using patch analysis. J Mol Biol 272: 133-143
    • (1997) J Mol Biol , vol.272 , pp. 133-143
    • Jones, S.1    Thornton, J.M.2
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47: 110-119
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • Katzen F, Beckwith J (2000) Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell 103: 769-779
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 30
    • 0042838288 scopus 로고    scopus 로고
    • Role and location of the unusual redoxactive cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD
    • Katzen F, Beckwith J (2003) Role and location of the unusual redoxactive cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD. Proc Natl Acad Sci USA 100: 10471-10476
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10471-10476
    • Katzen, F.1    Beckwith, J.2
  • 31
    • 0036682611 scopus 로고    scopus 로고
    • Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD
    • Katzen F, Deshmukh M, Daldal F, Beckwith J (2002) Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. EMBO J 21: 3960-3969
    • (2002) EMBO J , vol.21 , pp. 3960-3969
    • Katzen, F.1    Deshmukh, M.2    Daldal, F.3    Beckwith, J.4
  • 32
    • 0037716929 scopus 로고    scopus 로고
    • Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity
    • Kim JH, Kim SJ, Jeong DG, Son JH, Ryu SE (2003) Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity. FEBS Lett 543: 164-169
    • (2003) FEBS Lett , vol.543 , pp. 164-169
    • Kim, J.H.1    Kim, S.J.2    Jeong, D.G.3    Son, J.H.4    Ryu, S.E.5
  • 33
    • 0028948780 scopus 로고
    • Redox states of DsbA in the periplasm of Escherichia coli
    • Kishigami S, Akiyama Y, Ito K (1995) Redox states of DsbA in the periplasm of Escherichia coli. FEBS Lett 364: 55-58
    • (1995) FEBS Lett , vol.364 , pp. 55-58
    • Kishigami, S.1    Akiyama, Y.2    Ito, K.3
  • 34
    • 0030498233 scopus 로고    scopus 로고
    • xdIMAPMAN and xdIDATAMAN-programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets
    • Kleywegt GJ, Jones TA (1996) xdIMAPMAN and xdIDATAMAN-programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets. Acta Crystallogr D 52: 826-828
    • (1996) Acta Crystallogr D , vol.52 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 35
    • 0033106153 scopus 로고    scopus 로고
    • Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway
    • Kobayashi T, Ito K (1999) Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway. EMBO J 18: 1192-1198
    • (1999) EMBO J , vol.18 , pp. 1192-1198
    • Kobayashi, T.1    Ito, K.2
  • 36
    • 0035793545 scopus 로고    scopus 로고
    • DsbD-catalyzed transport of electrons across the membrane of Escherichia coli
    • Krupp R, Chan C, Missiakas D (2001) DsbD-catalyzed transport of electrons across the membrane of Escherichia coli. J Biol Chem 276: 3696-3701
    • (2001) J Biol Chem , vol.276 , pp. 3696-3701
    • Krupp, R.1    Chan, C.2    Missiakas, D.3
  • 38
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence MC, Colman PM (1993) Shape complementarity at protein/protein interfaces. J Mol Biol 234: 946-950
    • (1993) J Mol Biol , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 39
    • 0037229810 scopus 로고    scopus 로고
    • DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo
    • Maskos K, Huber-Wunderlich M, Glockshuber R (2003) DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo. J Mol Biol 325: 495-513
    • (2003) J Mol Biol , vol.325 , pp. 495-513
    • Maskos, K.1    Huber-Wunderlich, M.2    Glockshuber, R.3
  • 41
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • Missiakas D, Georgopoulos C, Raina S (1994) The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J 13: 2013-2020
    • (1994) EMBO J , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 42
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr A 50: 157-153
    • (1994) Acta Crystallogr A , vol.50 , pp. 157-153
    • Navaza, J.1
  • 43
    • 0028360184 scopus 로고
    • Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo
    • Nelson JW, Creighton TE (1994) Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry 33: 5974-5983
    • (1994) Biochemistry , vol.33 , pp. 5974-5983
    • Nelson, J.W.1    Creighton, T.E.2
  • 44
    • 0000732609 scopus 로고
    • GRASP graphical representation and analysis of surface properties
    • Nicholls A, Bharadwaj R, Honig B (1993) GRASP graphical representation and analysis of surface properties. Biophys J 64: A166
    • (1993) Biophys J , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 45
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-328
    • (1997) Methods Enzymol , vol.276 , pp. 307-328
    • Otwinowski, Z.1    Minor, W.2
  • 46
    • 0035311005 scopus 로고    scopus 로고
    • The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly
    • Reid E, Cole J, Eaves DJ (2001) The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly. Biochem J 355: 51-58
    • (2001) Biochem J , vol.355 , pp. 51-58
    • Reid, E.1    Cole, J.2    Eaves, D.J.3
  • 47
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch A, Bessette P, Georgiou G, Beckwith J (1997) Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J Bacteriol 179: 6602-6608
    • (1997) J Bacteriol , vol.179 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 48
    • 0034770083 scopus 로고    scopus 로고
    • Roles of thiol-redox pathways in bacteria
    • Ritz D, Beckwith J (2001) Roles of thiol-redox pathways in bacteria. Annu Rev Microbiol 55: 21-48
    • (2001) Annu Rev Microbiol , vol.55 , pp. 21-48
    • Ritz, D.1    Beckwith, J.2
  • 49
    • 0000519682 scopus 로고
    • Reduction-potential of glutathione
    • Rost J, Rapoport S (1964) Reduction-potential of glutathione. Nature 201: 185
    • (1964) Nature , vol.201 , pp. 185
    • Rost, J.1    Rapoport, S.2
  • 50
    • 0026781216 scopus 로고
    • Equilibrium and kinetic constants for the thiol-disulfide interchange reaction between glutathione and dithiothreitol
    • Rothwarf DM, Scheraga HA (1992) Equilibrium and kinetic constants for the thiol-disulfide interchange reaction between glutathione and dithiothreitol. Proc Natl Acad Sci USA 89: 7944-7948
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7944-7948
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 52
    • 0033230589 scopus 로고    scopus 로고
    • Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli
    • Stewart EJ, Katzen F, Beckwith J (1999) Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. EMBO J 18: 5963-5971
    • (1999) EMBO J , vol.18 , pp. 5963-5971
    • Stewart, E.J.1    Katzen, F.2    Beckwith, J.3
  • 53
    • 0034725691 scopus 로고    scopus 로고
    • The N-terminal sequence (residues 1-65) is essential for dimerization, activities, and peptide binding of Escherichia coli DsbC
    • Sun XX, Wang CC (2000) The N-terminal sequence (residues 1-65) is essential for dimerization, activities, and peptide binding of Escherichia coli DsbC. J Biol Chem 275: 22743-22749
    • (2000) J Biol Chem , vol.275 , pp. 22743-22749
    • Sun, X.X.1    Wang, C.C.2
  • 54
    • 33847087446 scopus 로고
    • Rate constants and equilibrium constants of thiol-disulfide interchange reactions involving oxidized glutathione
    • Szajewski RP, Whitesides GM (1980) Rate constants and equilibrium constants of thiol-disulfide interchange reactions involving oxidized glutathione. J Am Chem Soc 102: 2011-2026
    • (1980) J Am Chem Soc , vol.102 , pp. 2011-2026
    • Szajewski, R.P.1    Whitesides, G.M.2
  • 55
    • 0032577637 scopus 로고    scopus 로고
    • The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli
    • van Straaten M, Missiakas D, Raina S, Darby NJ (1998) The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli. FEBS Lett 428: 255-258
    • (1998) FEBS Lett , vol.428 , pp. 255-258
    • Van Straaten, M.1    Missiakas, D.2    Raina, S.3    Darby, N.J.4
  • 56
    • 0027366182 scopus 로고
    • Bacterial protein disulfide isomerase: Efficient catalysis of oxidative protein folding at acidic pH
    • Wunderlich M, Otto A, Seckler R, Glockshuber R (1993) Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH. Biochemistry 32: 12251-12256
    • (1993) Biochemistry , vol.32 , pp. 12251-12256
    • Wunderlich, M.1    Otto, A.2    Seckler, R.3    Glockshuber, R.4
  • 57
    • 0028222390 scopus 로고
    • Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin
    • Zapun A, Creighton TE (1994) Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin. Biochemistry 33: 5202-5211
    • (1994) Biochemistry , vol.33 , pp. 5202-5211
    • Zapun, A.1    Creighton, T.E.2
  • 58
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • Zapun A, Missiakas D, Raina S, Creighton TE (1995) Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34: 5075-5089
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2    Raina, S.3    Creighton, T.E.4


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