메뉴 건너뛰기




Volumn 12, Issue 8, 2010, Pages 921-931

Characterization of the DsbA oxidative folding catalyst from pseudomonas aeruginosa reveals a highly oxidizing protein that binds small molecules

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; DSBA PROTEIN; GLYCEROL; INSULIN; ISOMERASE;

EID: 77949599606     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2009.2736     Document Type: Article
Times cited : (27)

References (53)
  • 3
  • 4
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell JC, McGovern K, and Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell 67: 581-589, 1991.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 5
    • 34250348569 scopus 로고    scopus 로고
    • A combined approach to improving large-scale production of tobacco etch virus protease
    • Blommel PG and Fox BG. A combined approach to improving large-scale production of tobacco etch virus protease. Protein Expr Purif 55: 53-68, 2007.
    • (2007) Protein Expr Purif , vol.55 , pp. 53-68
    • Blommel, P.G.1    Fox, B.G.2
  • 7
    • 0035854737 scopus 로고    scopus 로고
    • Maturation of Pseudomonas aeruginosa elas-tase: Formation of the disulfide bonds
    • Braun P, Ockhuijsen C, Eppens E, Koster M, Bitter W, and Tommassen J. Maturation of Pseudomonas aeruginosa elas-tase: formation of the disulfide bonds. J Biol Chem 276: 26030-26035, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 26030-26035
    • Braun, P.1    Ockhuijsen, C.2    Eppens, E.3    Koster, M.4    Bitter, W.5    Tommassen, J.6
  • 8
    • 33750110911 scopus 로고    scopus 로고
    • The type III secretion injectisome
    • Cornelis GR. The type III secretion injectisome. Nat Rev Microbiol 4: 811-825, 2006.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 811-825
    • Cornelis, G.R.1
  • 10
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132, 2004.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 11
    • 0032479154 scopus 로고    scopus 로고
    • Protease IV,a unique extracellular protease and virulence factor from Pseudomonas aeruginosa
    • Engel LS, Hill JM, Caballero AR, Green LC, and O'Callaghan RJ. Protease IV, a unique extracellular protease and virulence factor from Pseudomonas aeruginosa. J Biol Chem 273: 16792-16797, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 16792-16797
    • Engel, L.S.1    Hill, J.M.2    Caballero, A.R.3    Green, L.C.4    O'Callaghan, R.J.5
  • 12
    • 0034769748 scopus 로고    scopus 로고
    • Prevalence of type III secretion genes in clinical and environmental isolates of Pseudomonas aeruginosa
    • Feltman H, Schulert G, Khan S, Jain M, Peterson L, and Hauser AR. Prevalence of type III secretion genes in clinical and environmental isolates of Pseudomonas aeruginosa. Microbiology 147: 2659-2669, 2001.
    • (2001) Microbiology , vol.147 , pp. 2659-2669
    • Feltman, H.1    Schulert, G.2    Khan, S.3    Jain, M.4    Peterson, L.5    Hauser, A.R.6
  • 13
    • 45549122242 scopus 로고    scopus 로고
    • DsbL and DsbI form a specific dithiol oxidase system for periplasmic aryl-sulfate sulfotransferase in uropathogenic Escherichia coli
    • Grimshaw JP, Stirnimann CU, Brozzo MS, Malojcic G, Grutter MG, Capitani G, and Glockshuber R. DsbL and DsbI form a specific dithiol oxidase system for periplasmic aryl-sulfate sulfotransferase in uropathogenic Escherichia coli. J Mol Biol 380: 667-680, 2008.
    • (2008) J Mol Biol , vol.380 , pp. 667-680
    • Grimshaw, J.P.1    Stirnimann, C.U.2    Brozzo, M.S.3    Malojcic, G.4    Grutter, M.G.5    Capitani, G.6    Glockshuber, R.7
  • 14
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, and Beckwith J. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177: 4121-4130, 1995.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 15
    • 0037372822 scopus 로고    scopus 로고
    • DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors
    • Ha UH, Wang Y, and Jin S. DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors. Infect Immun 71: 1590-1595, 2003.
    • (2003) Infect Immun , vol.71 , pp. 1590-1595
    • Ha, U.H.1    Wang, Y.2    Jin, S.3
  • 16
    • 0031000174 scopus 로고    scopus 로고
    • The type-4 pilus is the major virulence-associated adhesin of Pseudomonas aeruginosa: A review
    • Hahn HP. The type-4 pilus is the major virulence-associated adhesin of Pseudomonas aeruginosa: a review. Gene 192: 99-108, 1997.
    • (1997) Gene , vol.192 , pp. 99-108
    • Hahn, H.P.1
  • 19
    • 0021152329 scopus 로고
    • Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase
    • Hillson DA, Lambert N, and Freedman RB. Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase. Methods Enzymol 107: 281-294, 1984.
    • (1984) Methods Enzymol , vol.107 , pp. 281-294
    • Hillson, D.A.1    Lambert, N.2    Freedman, R.B.3
  • 20
  • 21
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A. Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254: 9627-9632, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 22
    • 0031585999 scopus 로고    scopus 로고
    • Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae
    • Hu SH, Peek JA, Rattigan E, Taylor RK, and Martin JL. Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae. J Mol Biol 268: 137-146, 1997.
    • (1997) J Mol Biol , vol.268 , pp. 137-146
    • Hu, S.H.1    Peek, J.A.2    Rattigan, E.3    Taylor, R.K.4    Martin, J.L.5
  • 23
    • 0031776171 scopus 로고    scopus 로고
    • A single dipep-tide sequence modulates the redox properties of a whole enzyme family
    • Huber-Wunderlich M, and Glockshuber R. A single dipep-tide sequence modulates the redox properties of a whole enzyme family. Fold Des 3: 161-171, 1998.
    • (1998) Fold des , vol.3 , pp. 161-171
    • Huber-Wunderlich, M.1    Glockshuber, R.2
  • 24
    • 33750813327 scopus 로고    scopus 로고
    • Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation
    • Inaba K, Murakami S, Suzuki M, Nakagawa A, Yamashita E, Okada K, and Ito K. Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127: 789-801, 2006.
    • (2006) Cell , vol.127 , pp. 789-801
    • Inaba, K.1    Murakami, S.2    Suzuki, M.3    Nakagawa, A.4    Yamashita, E.5    Okada, K.6    Ito, K.7
  • 25
    • 0037325617 scopus 로고    scopus 로고
    • Global epidemiology of antimicrobial resistance among community-acquired and nosocomial pathogens: A five-year summary from the SENTRY Antimicrobial Surveillance Program (997-2001)
    • Jones R. Global epidemiology of antimicrobial resistance among community-acquired and nosocomial pathogens: a five-year summary from the SENTRY Antimicrobial Surveillance Program (1997-2001). Semin Respir Crit Care Med 24: 121-134, 2003.
    • (2003) Semin Respir Crit Care Med , vol.24 , pp. 121-134
    • Jones, R.1
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637, 1983.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 69749094630 scopus 로고    scopus 로고
    • Biochemical and structural study of the homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis
    • Lafaye C, Iwema T, Carpentier P, Jullian-Binard C, Kroll JS, Collet JF, and Serre L. Biochemical and structural study of the homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis. J Mol Biol 392: 952-966, 2009.
    • (2009) J Mol Biol , vol.392 , pp. 952-966
    • Lafaye, C.1    Iwema, T.2    Carpentier, P.3    Jullian-Binard, C.4    Kroll, J.S.5    Collet, J.F.6    Serre, L.7
  • 29
    • 13444254300 scopus 로고    scopus 로고
    • PDBsum more: New summaries and analyses of the known 3D structures of proteins and nucleic acids
    • Laskowski RA, Chistyakov VV, and Thornton JM. PDBsum more: new summaries and analyses of the known 3D structures of proteins and nucleic acids. Nucleic Acids Res 33: D266-D268, 2005.
    • (2005) Nucleic Acids Res , vol.33
    • Laskowski, R.A.1    Chistyakov, V.V.2    Thornton, J.M.3
  • 30
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by Calpha geometry: Phi, psi and Cbeta deviation
    • Lovell SC, Davis IW, Arendall WB 3rd, de Bakker PI, Word JM, Prisant MG, Richardson JS, and Richardson DC. Structure validation by Calpha geometry: phi, psi and Cbeta deviation. Proteins 50: 437-450, 2003.
    • (2003) Proteins , vol.50 , pp. 437-450
    • Lovell, S.C.1
  • 31
    • 0024402268 scopus 로고
    • Effects of eliminating a disulfide bridge within domain II of Pseudomonas aeruginosa exotoxin A
    • Madshus IH and Collier RJ. Effects of eliminating a disulfide bridge within domain II of Pseudomonas aeruginosa exotoxin A. Infect Immun 57: 1873-1878, 1989.
    • (1989) Infect Immun , vol.57 , pp. 1873-1878
    • Madshus, I.H.1    Collier, R.J.2
  • 32
    • 0034459640 scopus 로고    scopus 로고
    • Pro-teome analysis of the effect of mucoid conversion on global protein expression in Pseudomonas aeruginosa strain PAO1 shows induction of the disulfide bond isomerase, DsbA
    • Malhotra S, Silo-Suh LA, Mathee K, and Ohman DE. Pro-teome analysis of the effect of mucoid conversion on global protein expression in Pseudomonas aeruginosa strain PAO1 shows induction of the disulfide bond isomerase, DsbA. J Bacteriol 182: 6999-7006, 2000.
    • (2000) J Bacteriol , vol.182 , pp. 6999-7006
    • Malhotra, S.1    Silo-Suh, L.A.2    Mathee, K.3    Ohman, D.E.4
  • 33
    • 0029165589 scopus 로고
    • Thioredoxin: A fold for all reasons
    • Martin JL. Thioredoxin: a fold for all reasons. Structure 3: 245-250, 1995.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 34
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin JL, Bardwell JC, and Kuriyan J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365: 464-468, 1993.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.2    Kuriyan, J.3
  • 35
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. Solvent content of protein crystals. J Mol Biol 33: 491-497, 1968.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 36
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D Biol Crystallogr 63: 32-41, 2007.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326, 1997.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131: 266-280, 1986.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 39
    • 52249094198 scopus 로고    scopus 로고
    • Microbiology: Desperately seeking new antibiotics
    • Payne DJ. Microbiology: desperately seeking new antibiotics. Science 321: 1644-1645, 2008.
    • (2008) Science , vol.321 , pp. 1644-1645
    • Payne, D.J.1
  • 40
    • 67349083918 scopus 로고    scopus 로고
    • Carbapenem-resistant Pseudomonas aeruginosa: Factors influencing multidrug-resistant acquisition in non-critically ill patients
    • Pena C, Suarez C, Tubau F, Dominguez A, Sora M, Pujol M, Gudiol F, and Ariza J. Carbapenem-resistant Pseudomonas aeruginosa: factors influencing multidrug-resistant acquisition in non-critically ill patients. Eur J Clin Microbiol Infect Dis 28: 519-522, 2009.
    • (2009) Eur J Clin Microbiol Infect Dis , vol.28 , pp. 519-522
    • Pena, C.1    Suarez, C.2    Tubau, F.3    Dominguez, A.4    Sora, M.5    Pujol, M.6    Gudiol, F.7    Ariza, J.8
  • 41
    • 0013815214 scopus 로고
    • Stereochemical criteria for polypeptide and protein chain conformations II. Allowed conformations for a pair of peptide units
    • Ramakrishnan C and Ramachandran GN. Stereochemical criteria for polypeptide and protein chain conformations, II. Allowed conformations for a pair of peptide units. Biophys J 5: 909-933, 1965.
    • (1965) Biophys J , vol.5 , pp. 909-933
    • Ramakrishnan, C.1    Ramachandran, G.N.2
  • 42
    • 0033023730 scopus 로고    scopus 로고
    • Nosocomial infections in medical intensive care units in the United States: National Nosocomial Infections Surveillance System
    • Richards MJ, Edwards JR, Culver DH, and Gaynes RP. Nosocomial infections in medical intensive care units in the United States: National Nosocomial Infections Surveillance System. Crit Care Med 27: 887-892, 1999.
    • (1999) Crit Care Med , vol.27 , pp. 887-892
    • Richards, M.J.1    Edwards, J.R.2    Culver, D.H.3    Gaynes, R.P.4
  • 43
    • 65249146593 scopus 로고    scopus 로고
    • Structural and biochemical characterization of Xylella fastidiosa DsbA family members: New insights into the enzyme-substrate interaction
    • Rinaldi FC, Meza AN, and Guimaraes BG. Structural and biochemical characterization of Xylella fastidiosa DsbA family members: new insights into the enzyme-substrate interaction. Biochemistry 48: 3508-3518, 2009.
    • (2009) Biochemistry , vol.48 , pp. 3508-3518
    • Rinaldi, F.C.1    Meza, A.N.2    Guimaraes, B.G.3
  • 44
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method, 1.Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro MM and Bolen DW. Unfolding free energy changes determined by the linear extrapolation method, 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27: 8063-8068, 1988.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 45
    • 4844227315 scopus 로고    scopus 로고
    • Functional diversity of three different DsbA proteins from Neisseria meningitidis
    • Sinha S, Langford PR, and Kroll JS. Functional diversity of three different DsbA proteins from Neisseria meningitidis. Microbiology 150: 2993-3000, 2004.
    • (2004) Microbiology , vol.150 , pp. 2993-3000
    • Sinha, S.1    Langford, P.R.2    Kroll, J.S.3
  • 46
    • 58949091766 scopus 로고    scopus 로고
    • Emergence of extensively drug-resistant and pandrug-resistant Gram-negative bacilli in Europe
    • Souli M, Galani I, and Giamarellou H. Emergence of extensively drug-resistant and pandrug-resistant Gram-negative bacilli in Europe. Euro Surveill 13: 1-11, 2008.
    • (2008) Euro Surveill , vol.13 , pp. 1-11
    • Souli, M.1    Galani, I.2    Giamarellou, H.3
  • 47
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW. Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41: 207-234, 2005.
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 48
    • 67549146965 scopus 로고    scopus 로고
    • Characterization of two homologous disulfide bond systems involved in virulence factor biogenesis in uro-pathogenic Escherichia coli CFT073
    • Totsika M, Heras B, Wurpel DJ, and Schembri MA. Characterization of two homologous disulfide bond systems involved in virulence factor biogenesis in uro-pathogenic Escherichia coli CFT073. J Bacteriol 191: 3901-3908, 2009.
    • (2009) J Bacteriol , vol.191 , pp. 3901-3908
    • Totsika, M.1    Heras, B.2    Wurpel, D.J.3    Schembri, M.A.4
  • 49
    • 0035150136 scopus 로고    scopus 로고
    • DsbA and DsbC affect extracellular enzyme formation in Pseudomonas aeruginosa
    • Urban A, Leipelt M, Eggert T, and Jaeger KE. DsbA and DsbC affect extracellular enzyme formation in Pseudomonas aeruginosa. J Bacteriol 183: 587-596, 2001.
    • (2001) J Bacteriol , vol.183 , pp. 587-596
    • Urban, A.1    Leipelt, M.2    Eggert, T.3    Jaeger, K.E.4
  • 51
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Wunderlich M and Glockshuber R. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci 2: 717-726, 1993.
    • (1993) Protein Sci , vol.2 , pp. 717-726
    • Wunderlich, M.1    Glockshuber, R.2
  • 52
    • 0027254133 scopus 로고
    • The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
    • Zapun A, Bardwell JC, and Creighton TE. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry 32: 5083-5092, 1993.
    • (1993) Biochemistry , vol.32 , pp. 5083-5092
    • Zapun, A.1    Bardwell, J.C.2    Creighton, T.E.3
  • 53
    • 17644392830 scopus 로고    scopus 로고
    • TM-align: A protein structure alignment algorithm based on the TM-score
    • Zhang Y and Skolnick J. TM-align: a protein structure alignment algorithm based on the TM-score. Nucleic Acids Res 33: 2302-2309, 2005.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2302-2309
    • Zhang, Y.1    Skolnick, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.