메뉴 건너뛰기




Volumn 289, Issue 5, 2014, Pages 2563-2576

The multidrug resistance IncA/C transferable plasmid encodes a novel domain-swapped dimeric protein-disulfide isomerase

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC RESISTANCE; BACTERIAL CONJUGATION; CRYSTAL STRUCTURE; DISULFIDE; DISULFIDE ISOMERASE; DOMAIN SWAPPING; DSBC/DSBG; ENZYME STRUCTURE; HORIZONTAL GENE TRANSFER; MULTIDRUG RESISTANCE;

EID: 84893484574     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.516898     Document Type: Article
Times cited : (7)

References (79)
  • 2
    • 80052247996 scopus 로고    scopus 로고
    • Emergence and rapid regional spread of Klebsiella pneumoniae carbapenemase-producing Enterobacteriaceae
    • Won, S. Y., Munoz-Price, L. S., Lolans, K., Hota, B., Weinstein, R. A., and Hayden, M. K. (2011) Emergence and rapid regional spread of Klebsiella pneumoniae carbapenemase-producing Enterobacteriaceae. Clin. Infect. Dis. 53, 532-540
    • (2011) Clin. Infect. Dis. , vol.53 , pp. 532-540
    • Won, S.Y.1    Munoz-Price, L.S.2    Lolans, K.3    Hota, B.4    Weinstein, R.A.5    Hayden, M.K.6
  • 3
    • 80051630584 scopus 로고    scopus 로고
    • Comparative genomics of multidrug resistance-encoding IncA/C plasmids from commensal and pathogenic Escherichia coli from multiple animal sources
    • Fernández-Alarcón, C, Singer, R. S., and Johnson, T. J. (2011) Comparative genomics of multidrug resistance-encoding IncA/C plasmids from commensal and pathogenic Escherichia coli from multiple animal sources. PLoS ONE 6, e23415
    • (2011) PLoS ONE , vol.6
    • Fernández-Alarcón, C.1    Singer, R.S.2    Johnson, T.J.3
  • 4
    • 84875181975 scopus 로고    scopus 로고
    • Global spread of antibiotic resistance. The example of New Delhi metallo-β-lactamase (NDM)-mediated carbapenem resistance
    • Johnson, A. P., and Woodford, N. (2013) Global spread of antibiotic resistance. The example of New Delhi metallo-β-lactamase (NDM)-mediated carbapenem resistance. J. Med. Microbiol. 62, 499-513
    • (2013) J. Med. Microbiol. , vol.62 , pp. 499-513
    • Johnson, A.P.1    Woodford, N.2
  • 6
    • 74249119814 scopus 로고    scopus 로고
    • Mobile antibiotic resistance encoding elements promote their own diversity
    • Garriss, G., Waldor, M. K., and Burrus, V. (2009) Mobile antibiotic resistance encoding elements promote their own diversity. PLoS Genet. 5, e1000775
    • (2009) PLoS Genet. , vol.5
    • Garriss, G.1    Waldor, M.K.2    Burrus, V.3
  • 7
    • 77955629924 scopus 로고    scopus 로고
    • The 2009 Garrod lecture. The evolution of antimicrobial resistance, a Darwinian perspective
    • Sykes, R. (2010) The 2009 Garrod lecture. The evolution of antimicrobial resistance, a Darwinian perspective. J. Antimicrob. Chemother. 65, 1842-1852
    • (2010) J. Antimicrob. Chemother. , vol.65 , pp. 1842-1852
    • Sykes, R.1
  • 8
    • 70349277187 scopus 로고    scopus 로고
    • The structural biology of type IV secretion systems
    • Fronzes, R., Christie, P. J., and Waksman, G. (2009) The structural biology of type IV secretion systems. Nat. Rev. Microbiol. 7, 703-714
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 703-714
    • Fronzes, R.1    Christie, P.J.2    Waksman, G.3
  • 10
    • 84881025514 scopus 로고    scopus 로고
    • Thioredoxin-like proteins in F and other plasmid systems
    • Hemmis, C. W., and Schildbach, J. F. (2013) Thioredoxin-like proteins in F and other plasmid systems. Plasmid 70, 168-189
    • (2013) Plasmid , vol.70 , pp. 168-189
    • Hemmis, C.W.1    Schildbach, J.F.2
  • 11
    • 0023370122 scopus 로고
    • Analysis of Escherichia coli K12 F factor transfer genes, traQ, trbA, and trbB
    • Wu, J. H., Moore, D., Lee, T., and Ippen-Ihler, K. (1987) Analysis of Escherichia coli K12 F factor transfer genes, traQ, trbA, and trbB. Plasmid 18, 54-69
    • (1987) Plasmid , vol.18 , pp. 54-69
    • Wu, J.H.1    Moore, D.2    Lee, T.3    Ippen-Ihler, K.4
  • 12
    • 28844446587 scopus 로고    scopus 로고
    • F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues
    • Elton, T. C., Holland, S. J., Frost, L. S., and Hazes, B. (2005) F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues. J. Bacteriol. 187, 8267-8277
    • (2005) J. Bacteriol. , vol.187 , pp. 8267-8277
    • Elton, T.C.1    Holland, S.J.2    Frost, L.S.3    Hazes, B.4
  • 13
    • 80052536012 scopus 로고    scopus 로고
    • TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance
    • Hemmis, C. W., Berkmen, M., Eser, M., and Schildbach, J. F. (2011) TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance. J. Bacteriol. 193, 4588-4597
    • (2011) J. Bacteriol. , vol.193 , pp. 4588-4597
    • Hemmis, C.W.1    Berkmen, M.2    Eser, M.3    Schildbach, J.F.4
  • 19
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • Kadokura, H., Katzen, F., and Beckwith, J. (2003) Protein disulfide bond formation in prokaryotes. Annu. Rev. Biochem. 72, 111-135
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 20
    • 70449674774 scopus 로고    scopus 로고
    • Disulfide bond formation system in Escherichia coli
    • Inaba, K. (2009) Disulfide bond formation system in Escherichia coli. J. Biochem. 146, 591-597
    • (2009) J. Biochem. , vol.146 , pp. 591-597
    • Inaba, K.1
  • 21
    • 49649088871 scopus 로고    scopus 로고
    • Effects of substitutions in the CXXC active-site motif of the extracytoplasmic thioredoxin ResA
    • Lewin, A., Crow, A., Hodson, C. T., Hederstedt, L., and Le Brun, N. E. (2008) Effects of substitutions in the CXXC active-site motif of the extracytoplasmic thioredoxin ResA. Biochem. J. 414, 81-91
    • (2008) Biochem. J. , vol.414 , pp. 81-91
    • Lewin, A.1    Crow, A.2    Hodson, C.T.3    Hederstedt, L.4    Le Brun, N.E.5
  • 22
    • 84888117308 scopus 로고    scopus 로고
    • IncA/C plasmids. An emerging threat to human and animal health?
    • Johnson, T. J., and Lang, K. S. (2012) IncA/C plasmids. An emerging threat to human and animal health? Mob. Genet. Elements 2, 55-58
    • (2012) Mob. Genet. Elements , vol.2 , pp. 55-58
    • Johnson, T.J.1    Lang, K.S.2
  • 23
    • 0015030747 scopus 로고
    • Detection of resistance factors in fish pathogen Aeromonas liquefaciens
    • Aoki, T., Egusa, S., Ogata, Y., and Watanabe, T. (1971) Detection of resistance factors in fish pathogen Aeromonas liquefaciens. J. Gen. Microbiol. 65, 343-349
    • (1971) J. Gen. Microbiol. , vol.65 , pp. 343-349
    • Aoki, T.1    Egusa, S.2    Ogata, Y.3    Watanabe, T.4
  • 25
    • 84856074698 scopus 로고    scopus 로고
    • Evolution of IncA/C blaCMY-(2)-carrying plasmids by acquisition of the blaNDM-(1) carbapenemase gene
    • Carattoli, A., Villa, L., Poirel, L., Bonnin, R. A., and Nordmann, P. (2012) Evolution of IncA/C blaCMY-(2)-carrying plasmids by acquisition of the blaNDM-(1) carbapenemase gene. Antimicrob. Agents Chemother. 56, 783-786
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 783-786
    • Carattoli, A.1    Villa, L.2    Poirel, L.3    Bonnin, R.A.4    Nordmann, P.5
  • 26
    • 80053118752 scopus 로고    scopus 로고
    • Complete sequencing ofthe bla (NDM-1)-positive IncA/C plasmid from Escherichia coli ST38 isolate suggests a possible origin from plant pathogens
    • Sekizuka, T., Matsui, M., Yamane, K., Takeuchi, F., Ohnishi, M., Hishinuma, A., Arakawa, Y., and Kuroda, M. (2011) Complete sequencing ofthe bla (NDM-1)-positive IncA/C plasmid from Escherichia coli ST38 isolate suggests a possible origin from plant pathogens. PLoS ONE 6, e25334
    • (2011) PLoS ONE , vol.6
    • Sekizuka, T.1    Matsui, M.2    Yamane, K.3    Takeuchi, F.4    Ohnishi, M.5    Hishinuma, A.6    Arakawa, Y.7    Kuroda, M.8
  • 27
    • 84871208766 scopus 로고    scopus 로고
    • Complete nucleotide sequence of the large conjugative pTC2 multireplicon plasmid encoding the VIM-1 metallo-β-lactamase
    • Drieux, L., Decré, D., Frangeul, L., Arlet, G., Jarlier, V., and Sougakoff, W. (2013) Complete nucleotide sequence of the large conjugative pTC2 multireplicon plasmid encoding the VIM-1 metallo-β-lactamase. J. Antimicrob. Chemother. 68, 97-100
    • (2013) J. Antimicrob. Chemother. , vol.68 , pp. 97-100
    • Drieux, L.1    Decré, D.2    Frangeul, L.3    Arlet, G.4    Jarlier, V.5    Sougakoff, W.6
  • 28
    • 0036926615 scopus 로고    scopus 로고
    • A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site
    • Stols, L., Gu, M., Dieckman, L., Raffen, R., Collart, F. R., and Donnelly, M. I. (2002) A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Expr. Purif. 25, 8-15
    • (2002) Protein Expr. Purif. , vol.25 , pp. 8-15
    • Stols, L.1    Gu, M.2    Dieckman, L.3    Raffen, R.4    Collart, F.R.5    Donnelly, M.I.6
  • 29
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F. W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41, 207-234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 30
    • 0032562757 scopus 로고    scopus 로고
    • Reconstitution of a protein disulfide catalytic system
    • Bader, M., Muse, W., Zander, T., and Bardwell, J. (1998) Reconstitution of a protein disulfide catalytic system. J. Biol. Chem. 273, 10302-10307
    • (1998) J. Biol. Chem. , vol.273 , pp. 10302-10307
    • Bader, M.1    Muse, W.2    Zander, T.3    Bardwell, J.4
  • 33
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and postrefinement
    • Kabsch, W. (2010) Integration, scaling, space-group assignment and postrefinement. Acta Crystallogr. D Biol. Crystallogr. 66, 133-144
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 36
  • 40
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK. A unified set of procedures for evaluating the quality of macromolecular structurefactor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J., and Wodak, S. J. (1999) SFCHECK. A unified set of procedures for evaluating the quality of macromolecular structurefactor data and their agreement with the atomic model. Acta Crystallogr. D Biol. Crystallogr. 55, 191-205
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 41
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J. C, McGovern, K., and Beckwith, J. (1991) Identification of a protein required for disulfide bond formation in vivo. Cell 67, 581-589
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 42
    • 0021152329 scopus 로고
    • Formation and isomerization of disulfide bonds in proteins. Protein disulfide-isomerase
    • Hillson, D. A., Lambert, N., and Freedman, R. B. (1984) Formation and isomerization of disulfide bonds in proteins. Protein disulfide-isomerase. Methods Enzymol. 107, 281-294
    • (1984) Methods Enzymol. , vol.107 , pp. 281-294
    • Hillson, D.A.1    Lambert, N.2    Freedman, R.B.3
  • 45
    • 0037013828 scopus 로고    scopus 로고
    • Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade
    • Inaba, K., and Ito, K. (2002) Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade. EMBOJ. 21, 2646-2654
    • (2002) EMBOJ , vol.21 , pp. 2646-2654
    • Inaba, K.1    Ito, K.2
  • 46
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to Image J. 25 years of image analysis
    • Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. (2012) NIH Image to Image J. 25 years of image analysis. Nat Methods 9, 671-675
    • (2012) Nat Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 47
    • 0027436420 scopus 로고
    • In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfideisomerase (DsbA)
    • Wunderlich, M., and Glockshuber, R. (1993) In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfideisomerase (DsbA). J. Biol. Chem. 268, 24547-24550
    • (1993) J. Biol. Chem. , vol.268 , pp. 24547-24550
    • Wunderlich, M.1    Glockshuber, R.2
  • 48
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfide bond stability
    • Gilbert, H. F. (1995) Thiol/disulfide exchange equilibria and disulfide bond stability. Methods Enzymol. 251, 8-28
    • (1995) Methods Enzymol. , vol.251 , pp. 8-28
    • Gilbert, H.F.1
  • 49
    • 33947494479 scopus 로고    scopus 로고
    • Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG
    • Yeh, S. M., Koon, N., Squire, C, and Metcalf, P. (2007) Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG. Acta Crystallogr. D Biol. Crystallogr. 63, 465-471
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 465-471
    • Yeh, S.M.1    Koon, N.2    Squire, C.3    Metcalf, P.4
  • 51
    • 84879880557 scopus 로고    scopus 로고
    • Crystal structure of the periplasmic disulfide-bond isomerase DsbC from Salmonella enterica serovar Typhimurium and the mechanistic implications
    • Jiao, L., Kim, J. S., Song, W. S., Yoon, B. Y., Lee, K., and Ha, N. C (2013) Crystal structure of the periplasmic disulfide-bond isomerase DsbC from Salmonella enterica serovar Typhimurium and the mechanistic implications. J. Struct. Biol. 183, 1-10
    • (2013) J. Struct. Biol. , vol.183 , pp. 1-10
    • Jiao, L.1    Kim, J.S.2    Song, W.S.3    Yoon, B.Y.4    Lee, K.5    Ha, N.C.6
  • 52
    • 0030596062 scopus 로고    scopus 로고
    • Crystal structure of Arabidopsis thaliana NADPH-dependent thioredoxin reductase at 2. 5-Å resolution
    • Dai, S., Saarinen, M., Ramaswamy, S., Meyer, Y., Jacquot, J. P., and Eklund, H. (1996) Crystal structure of Arabidopsis thaliana NADPH-dependent thioredoxin reductase at 2. 5-Å resolution. J. Mol. Biol. 264, 1044-1057
    • (1996) J. Mol. Biol. , vol.264 , pp. 1044-1057
    • Dai, S.1    Saarinen, M.2    Ramaswamy, S.3    Meyer, Y.4    Jacquot, J.P.5    Eklund, H.6
  • 54
    • 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., and Creighton, T. E. (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
  • 55
    • 0033583239 scopus 로고    scopus 로고
    • In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
    • Bessette, P. H, Cotto, J. J., Gilbert, H. F., and 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
  • 57
    • 69949177419 scopus 로고    scopus 로고
    • Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC
    • Arredondo, S. A., Chen, T. F., Riggs, A. F., Gilbert, H. F., and Georgiou, G. (2009) Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC. J. Biol. Chem. 284, 23972-23979
    • (2009) J. Biol. Chem. , vol.284 , pp. 23972-23979
    • Arredondo, S.A.1    Chen, T.F.2    Riggs, A.F.3    Gilbert, H.F.4    Georgiou, G.5
  • 58
    • 0034691077 scopus 로고    scopus 로고
    • Bacteria are different. Observations, interpretations, speculations, and opinions about the mechanisms of adaptive evolution in prokaryotes
    • Levin, B. R., and Bergstrom, C. T. (2000) Bacteria are different. Observations, interpretations, speculations, and opinions about the mechanisms of adaptive evolution in prokaryotes. Proc. Natl. Acad. Sci. U. S. A. 97, 6981-6985
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6981-6985
    • Levin, B.R.1    Bergstrom, C.T.2
  • 59
    • 0033972854 scopus 로고    scopus 로고
    • Genetic variation. Molecular mechanisms and impact on microbial evolution
    • Arber, W. (2000) Genetic variation. Molecular mechanisms and impact on microbial evolution. FEMS Microbiol. Rev. 24, 1-7
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 1-7
    • Arber, W.1
  • 60
    • 0026760182 scopus 로고
    • The crisis in antibiotic resistance
    • Neu, H. C. (1992) The crisis in antibiotic resistance. Science 257, 1064-1073
    • (1992) Science , vol.257 , pp. 1064-1073
    • Neu, H.C.1
  • 61
    • 0033514493 scopus 로고    scopus 로고
    • The relationship between the volume of antimicrobial consumption in human communities and the frequency of resistance
    • Austin, D. J., Kristinsson, K. G., and Anderson, R. M. (1999) The relationship between the volume of antimicrobial consumption in human communities and the frequency of resistance. Proc. Natl. Acad. Sci. U. S. A. 96, 1152-1156
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 1152-1156
    • Austin, D.J.1    Kristinsson, K.G.2    Anderson, R.M.3
  • 62
    • 22544457611 scopus 로고    scopus 로고
    • A systematic review and meta-analysis of misuse of antibiotic therapies in the community
    • Kardas, P., Devine, S., Golembesky, A., and Roberts, C. (2005) A systematic review and meta-analysis of misuse of antibiotic therapies in the community. Int. J. Antimicrob. Agents 26, 106-113
    • (2005) Int. J. Antimicrob. Agents , vol.26 , pp. 106-113
    • Kardas, P.1    Devine, S.2    Golembesky, A.3    Roberts, C.4
  • 63
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping. As domains continue to swap
    • Liu, Y., and Eisenberg, D. (2002) 3D domain swapping. As domains continue to swap. Protein Sci. 11, 1285-1299
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 65
    • 0242353305 scopus 로고    scopus 로고
    • Dimerization by domain hybridization bestows chaperone and isomerase activities
    • Zhao, Z., Peng, Y., Hao, S. F., Zeng, Z. H, and Wang, C. C. (2003) Dimerization by domain hybridization bestows chaperone and isomerase activities. J. Biol. Chem. 278, 43292-43298
    • (2003) J. Biol. Chem. , vol.278 , pp. 43292-43298
    • Zhao, Z.1    Peng, Y.2    Hao, S.F.3    Zeng, Z.H.4    Wang, C.C.5
  • 66
    • 33646205345 scopus 로고    scopus 로고
    • Conserved role of the linker a-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB
    • Segatori, L., Murphy, L., Arredondo, S., Kadokura, H, Gilbert, H, Beckwith, J., and Georgiou, G. (2006) Conserved role of the linker a-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. J. Biol. Chem. 281, 4911-4919
    • (2006) J. Biol. Chem. , vol.281 , pp. 4911-4919
    • Segatori, L.1    Murphy, L.2    Arredondo, S.3    Kadokura, H.4    Gilbert, H.5    Beckwith, J.6    Georgiou, G.7
  • 67
    • 84878866786 scopus 로고    scopus 로고
    • Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase
    • Wang, C, Li, W., Ren, J., Fang, J., Ke, H., Gong, W., Feng, W., and Wang, C. C. (2013) Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase. Antioxid. Redox Signal. 19, 36-45
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 36-45
    • Wang, C.1    Li, W.2    Ren, J.3    Fang, J.4    Ke, H.5    Gong, W.6    Feng, W.7    Wang, C.C.8
  • 68
    • 0035151833 scopus 로고    scopus 로고
    • Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli
    • Bessette, P. H., Qiu, J., Bardwell, J. C, Swartz, J. R., and Georgiou, G. (2001) Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli. J. Bacteriol. 183, 980-988
    • (2001) J. Bacteriol. , vol.183 , pp. 980-988
    • Bessette, P.H.1    Qiu, J.2    Bardwell, J.C.3    Swartz, J.R.4    Georgiou, G.5
  • 70
    • 34250206320 scopus 로고    scopus 로고
    • A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteins
    • Su, D., Berndt, C., Fomenko, D. E., Holmgren, A., and Gladyshev, V. N. (2007) A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteins. Biochemistry 46, 6903-6910
    • (2007) Biochemistry , vol.46 , pp. 6903-6910
    • Su, D.1    Berndt, C.2    Fomenko, D.E.3    Holmgren, A.4    Gladyshev, V.N.5
  • 71
    • 0030880594 scopus 로고    scopus 로고
    • Structural analysis of three His32 mutants of DsbA. Support for an electrostatic role of His32 in DsbA stability
    • Guddat, L. W., Bardwell, J. C., Glockshuber, R., Huber-Wunderlich, M., Zander, T., and Martin, J. L. (1997) Structural analysis of three His32 mutants of DsbA. Support for an electrostatic role of His32 in DsbA stability. Protein Sci. 6, 1893-1900
    • (1997) Protein Sci. , vol.6 , pp. 1893-1900
    • Guddat, L.W.1    Bardwell, J.C.2    Glockshuber, R.3    Huber-Wunderlich, M.4    Zander, T.5    Martin, J.L.6
  • 72
    • 0039714219 scopus 로고    scopus 로고
    • Characterization of Escherichia coli thioredoxin variants mimicking the activesites of other thiol/disulfide oxidoreductases
    • Mössner, E., Huber-Wunderlich, M., and Glockshuber, R. (1998) Characterization of Escherichia coli thioredoxin variants mimicking the activesites of other thiol/disulfide oxidoreductases. Protein Sci. 7, 1233-1244
    • (1998) Protein Sci. , vol.7 , pp. 1233-1244
    • Mössner, E.1    Huber-Wunderlich, M.2    Glockshuber, R.3
  • 74
    • 0037309117 scopus 로고    scopus 로고
    • Characterization of SrgA, a Salmonella enterica serovar Typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae
    • Bouwman, C. W., Kohli, M., Killoran, A., Touchie, G. A., Kadner, R. J., and Martin, N. L. (2003) Characterization of SrgA, a Salmonella enterica serovar Typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae. J. Bacteriol. 185, 991-1000
    • (2003) J. Bacteriol. , vol.185 , pp. 991-1000
    • Bouwman, C.W.1    Kohli, M.2    Killoran, A.3    Touchie, G.A.4    Kadner, R.J.5    Martin, N.L.6
  • 77
    • 1842477219 scopus 로고    scopus 로고
    • In vivo substrate specificity of periplasmic disulfide oxidoreductases
    • Hiniker, A., and Bardwell, J. C. (2004) In vivo substrate specificity of periplasmic disulfide oxidoreductases. J. Biol. Chem. 279, 12967-12973
    • (2004) J. Biol. Chem. , vol.279 , pp. 12967-12973
    • Hiniker, A.1    Bardwell, J.C.2
  • 78
    • 1642556877 scopus 로고    scopus 로고
    • Snapshots of DsbA in action. Detection of proteins in the process of oxidative folding
    • Kadokura, H., Tian, H., Zander, T., Bardwell, J. C., and Beckwith, J. (2004) Snapshots of DsbA in action. Detection of proteins in the process of oxidative folding. Science 303, 534-537
    • (2004) Science , vol.303 , pp. 534-537
    • Kadokura, H.1    Tian, H.2    Zander, T.3    Bardwell, J.C.4    Beckwith, J.5
  • 79
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.