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Volumn 13, Issue 1, 2013, Pages

Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis

Author keywords

Disulfide bond; DsbA; Mycobacterium tuberculosis; Oxidoreductase; Vitamin K epoxide reductase; X ray crystallography

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; DSBA PROTEIN; DSBE PROTEIN; DSBF PROTEIN; ISOMERASE; THIOREDOXIN; UNCLASSIFIED DRUG; VKOR PROTEIN;

EID: 84885496417     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-13-23     Document Type: Article
Times cited : (30)

References (61)
  • 1
    • 78149469953 scopus 로고    scopus 로고
    • Multiple catalytically active thioredoxin folds: A winning strategy for many functions
    • Multiple catalytically active thioredoxin folds: a winning strategy for many functions. Pedone E, Limauro D, D'Ambrosio K, De Simone G, Bartolucci S, Cell Mol Life Sci 2010 67 3797 3814
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3797-3814
    • Pedone, E.1    Limauro, D.2    D'Ambrosio, K.3    De Simone, G.4    Bartolucci, S.5
  • 2
    • 41449093101 scopus 로고    scopus 로고
    • Disulfide bond isomerization in prokaryotes
    • Disulfide bond isomerization in prokaryotes. Gleiter S, Bardwell JC, Biochim Biophys Acta 2008 1783 530 534
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 530-534
    • Gleiter, S.1    Bardwell, J.C.2
  • 3
    • 33746298040 scopus 로고    scopus 로고
    • Protein disulfide isomerase: The structure of oxidative folding
    • DOI 10.1016/j.tibs.2006.06.001, PII S0968000406001459
    • Protein disulfide isomerase: the structure of oxidative folding. Gruber CW, Cemazar M, Heras B, Martin JL, Craik DJ, Trends Biochem Sci 2006 31 455 464 (Pubitemid 44108657)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.8 , pp. 455-464
    • Gruber, C.W.1    Cemazar, M.2    Heras, B.3    Martin, J.L.4    Craik, D.J.5
  • 4
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Protein folding in the bacterial periplasm. Missiakas D, Raina S, J Bacteriol 1997 179 2465 2471 (Pubitemid 27164541)
    • (1997) Journal of Bacteriology , vol.179 , Issue.8 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 5
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Identification of a protein required for disulfide bond formation in vivo. Bardwell JC, McGovern K, Beckwith J, Cell 1991 67 581 589 (Pubitemid 121001472)
    • (1991) Cell , vol.67 , Issue.3 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 6
    • 0030787850 scopus 로고    scopus 로고
    • In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC
    • DOI 10.1021/bi9707739
    • In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. Joly JC, Swartz JR, Biochemistry 1997 36 10067 10072 (Pubitemid 27357714)
    • (1997) Biochemistry , vol.36 , Issue.33 , pp. 10067-10072
    • Joly, J.C.1    Swartz, J.R.2
  • 7
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • DOI 10.1016/S0092-8674(00)81016-8
    • Oxidative protein folding is driven by the electron transport system. Bader M, Muse W, Ballou DP, Gassner C, Bardwell JC, Cell 1999 98 217 227 (Pubitemid 29344909)
    • (1999) Cell , vol.98 , Issue.2 , pp. 217-227
    • Bader, M.1    Muse, W.2    Ballou, D.P.3    Gassner, C.4    Bardwell, J.C.A.5
  • 9
    • 0033583239 scopus 로고    scopus 로고
    • In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
    • In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG. Bessette PH, Cotto JJ, Gilbert HF, Georgiou G, J Biol Chem 1999 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
  • 10
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. Rietsch A, Bessette P, Georgiou G, Beckwith J, J Bacteriol 1997 179 6602 6608 (Pubitemid 27465291)
    • (1997) Journal of Bacteriology , vol.179 , Issue.21 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 11
    • 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
    • DOI 10.1093/emboj/18.21.5963
    • 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, EMBO J 1999 18 5963 5971 (Pubitemid 29515673)
    • (1999) EMBO Journal , vol.18 , Issue.21 , pp. 5963-5971
    • Stewart, E.J.1    Katzen, F.2    Beckwith, J.3
  • 12
    • 0029843893 scopus 로고    scopus 로고
    • The role of the genes nrf EFG and ccmFH in cytochrome c biosynthesis in Escherichia coli
    • The role of the genes nrf EFG and ccmFH in cytochrome c biosynthesis in Escherichia coli. Grovc J, Busby S, Cole J, Mol Gen Genet 1996 252 332 341
    • (1996) Mol Gen Genet , vol.252 , pp. 332-341
    • Grovc, J.1    Busby, S.2    Cole, J.3
  • 13
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Bessette PH, Aslund F, Beckwith J, Georgiou G, Proc Natl Acad Sci USA 1999 96 13703 13708
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 16
    • 0032786363 scopus 로고    scopus 로고
    • DsbA: A protein-folding catalyst contributing to bacterial virulence
    • DsbA: a protein-folding catalyst contributing to bacterial virulence. Yu J, Kroll JS, Microbes Infect 1999 1 1221 1228
    • (1999) Microbes Infect , vol.1 , pp. 1221-1228
    • Yu, J.1    Kroll, J.S.2
  • 17
  • 18
    • 0030957263 scopus 로고    scopus 로고
    • The tcp gene cluster of Vibrio cholerae
    • DOI 10.1016/S0378-1119(97)00036-X, PII S037811199700036X
    • The tcp gene cluster of Vibrio cholerae. Manning PA, Gene 1997 192 63 70 (Pubitemid 27267480)
    • (1997) Gene , vol.192 , Issue.1 , pp. 63-70
    • Manning, P.A.1
  • 19
    • 0029774730 scopus 로고    scopus 로고
    • DsbA is required for stability of the type IV pilin of enteropathogenic Escherichia coli
    • DsbA is required for stability of the type IV pilin of enteropathogenic Escherichia coli. Zhang HZ, Donnenberg MS, Mol Microbiol 1996 21 787 797 (Pubitemid 26281526)
    • (1996) Molecular Microbiology , vol.21 , Issue.4 , pp. 787-797
    • Zhang, H.-Z.1    Donnenberg, M.S.2
  • 20
    • 84887017364 scopus 로고    scopus 로고
    • The World Health Organization, Tuberculosis Global Control Facts http://www.who.int/tb/publications/global-report/2011/gtbr11-full.pdf
    • Tuberculosis Global Control Facts
  • 21
    • 0942287201 scopus 로고    scopus 로고
    • Gram-positive DsbE proteins function differently from gram-negative DsbE homologs: A structure to function analysis of DsbE from mycobacterium tuberculosis
    • DOI 10.1074/jbc.M311833200
    • Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis. Goulding CW, Apostol MI, Gleiter S, Parseghian A, Bardwell J, Gennaro M, Eisenberg D, J Biol Chem 2004 279 3516 3524 (Pubitemid 38140591)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3516-3524
    • Goulding, C.W.1    Apostol, M.I.2    Gleiter, S.3    Parseghian, A.4    Bardwell, J.5    Gennaro, M.6    Eisenberg, D.7
  • 23
    • 26444518218 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL regulates polyketide synthases and secreted or membrane proteins and is required for virulence
    • DOI 10.1128/JB.187.20.7062-7071.2005
    • The Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL regulates polyketide synthases and secreted or membrane proteins and is required for virulence. Hahn MY, Raman S, Anaya M, Husson RN, J Bacteriol 2005 187 7062 7071 (Pubitemid 41428883)
    • (2005) Journal of Bacteriology , vol.187 , Issue.20 , pp. 7062-7071
    • Hahn, M.-Y.1    Raman, S.2    Anaya, M.3    Husson, R.N.4
  • 24
    • 0034805873 scopus 로고    scopus 로고
    • Biochemical characterization of the thioredoxin domain of Escherichia coli DsbE protein reveals a weak reductant
    • DOI 10.1006/bbrc.2001.4876
    • Biochemical characterization of the thioredoxin domain of Escherichia coli DsbE protein reveals a weak reductant. Li Q, Hu H, Xu G, Biochem Biophys Res Commun 2001 283 849 853 (Pubitemid 32924657)
    • (2001) Biochemical and Biophysical Research Communications , vol.283 , Issue.4 , pp. 849-853
    • Li, Q.1    Hu, H.-Y.2    Xu, G.-J.3
  • 26
    • 50149109183 scopus 로고    scopus 로고
    • Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation
    • Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. Dutton RJ, Boyd D, Berkmen M, Beckwith J, Proc Natl Acad Sci USA 2008 105 11933 11938
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11933-11938
    • Dutton, R.J.1    Boyd, D.2    Berkmen, M.3    Beckwith, J.4
  • 28
    • 79952821270 scopus 로고    scopus 로고
    • Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase
    • Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase. Wang X, Dutton RJ, Beckwith J, Boyd D, Antioxid Redox Signal 2011 14 1413 1420
    • (2011) Antioxid Redox Signal , vol.14 , pp. 1413-1420
    • Wang, X.1    Dutton, R.J.2    Beckwith, J.3    Boyd, D.4
  • 30
    • 69949125089 scopus 로고    scopus 로고
    • Crystal structure and biophysical properties of Bacillus subtilis BdbD. An oxidizing thiol:Disulfide oxidoreductase containing a novel metal site
    • Crystal structure and biophysical properties of Bacillus subtilis BdbD. An oxidizing thiol:disulfide oxidoreductase containing a novel metal site. Crow A, Lewin A, Hecht O, Carlsson Moller M, Moore GR, Hederstedt L, Le Brun NE, J Biol Chem 2009 284 23719 23733
    • (2009) J Biol Chem , vol.284 , pp. 23719-23733
    • Crow, A.1    Lewin, A.2    Hecht, O.3    Carlsson Moller, M.4    Moore, G.R.5    Hederstedt, L.6    Le Brun, N.E.7
  • 34
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • DOI 10.1046/j.1365-2958.2003.03425.x
    • Genes required for mycobacterial growth defined by high density mutagenesis. Sassetti CM, Boyd DH, Rubin EJ, Mol Microbiol 2003 48 77 84 (Pubitemid 36411469)
    • (2003) Molecular Microbiology , vol.48 , Issue.1 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 35
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Wunderlich M, Glockshuber R, Protein Sci 1993 2 717 726 (Pubitemid 23121086)
    • (1993) Protein Science , vol.2 , Issue.5 , pp. 717-726
    • Wunderlich, M.1    Glockshuber, R.2
  • 36
    • 0027254133 scopus 로고
    • The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
    • DOI 10.1021/bi00070a016
    • The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Zapun A, Bardwell JC, Creighton TE, Biochemistry 1993 32 5083 5092 (Pubitemid 23162074)
    • (1993) Biochemistry , vol.32 , Issue.19 , pp. 5083-5092
    • Zapun, A.1    Bardwell, J.C.A.2    Creighton, T.E.3
  • 37
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • DOI 10.1016/j.jmb.2004.05.028, PII S0022283604005972
    • Improved prediction of signal peptides: signalP 3.0. Bendtsen JD, Nielsen H, von Heijne G, Brunak S, J Mol Biol 2004 340 783 795 (Pubitemid 38829638)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 38
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. Krogh A, Larsson B, von Heijne G, Sonnhammer EL, J Mol Biol 2001 305 567 580 (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 40
    • 0032526690 scopus 로고    scopus 로고
    • Crystal structures of reduced and oxidized DsbA: Investigation of domain motion and thiolate stabilization
    • Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization. Guddat LW, Bardwell JC, Martin JL, Structure 1998 6 757 767 (Pubitemid 28301209)
    • (1998) Structure , vol.6 , Issue.6 , pp. 757-767
    • Guddat, L.W.1    Bardwell, J.C.A.2    Martin, J.L.3
  • 41
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • DOI 10.1093/bioinformatics/btn507
    • Searching protein structure databases with DaliLite v.3. Holm L, Kaariainen S, Rosenstrom P, Schenkel A, Bioinform (Oxford, England) 2008 24 2780 2781 (Pubitemid 352722625)
    • (2008) Bioinformatics , vol.24 , Issue.23 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 44
    • 33750813327 scopus 로고    scopus 로고
    • Crystal Structure of the DsbB-DsbA Complex Reveals a Mechanism of Disulfide Bond Generation
    • DOI 10.1016/j.cell.2006.10.034, PII S0092867406014127
    • 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, Ito K, Cell 2006 127 789 801 (Pubitemid 44716258)
    • (2006) Cell , vol.127 , Issue.4 , pp. 789-801
    • Inaba, K.1    Murakami, S.2    Suzuki, M.3    Nakagawa, A.4    Yamashita, E.5    Okada, K.6    Ito, K.7
  • 47
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • DOI 10.1038/365464a0
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Martin JL, Bardwell JC, Kuriyan J, Nature 1993 365 464 468 (Pubitemid 23311046)
    • (1993) Nature , vol.365 , Issue.6445 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.A.2    Kuriyan, J.3
  • 51
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Arnold K, Bordoli L, Kopp J, Schwede T, Bioinformatics 2006 22 195 201 (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 54
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • A short history of SHELX. Sheldrick GM, Acta Crystallogr A 2008 64 112 122
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 58
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • DOI 10.1006/jmbi.1993.1351
    • Main-chain bond lengths and bond angles in protein structures. Laskowski RA, Moss DS, Thornton JM, J Mol Biol 1993 231 1049 1067 (Pubitemid 23209879)
    • (1993) Journal of Molecular Biology , vol.231 , Issue.4 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 59
    • 0027180507 scopus 로고
    • Verification of protein structures: Patterns of nonbonded atomic interactions
    • Verification of protein structures: patterns of nonbonded atomic interactions. Colovos C, Yeates TO, Protein Sci 1993 2 1511 1519 (Pubitemid 23262844)
    • (1993) Protein Science , vol.2 , Issue.9 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 60
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. Holmgren A, J Biol Chem 1979 254 9627 9632 (Pubitemid 10248727)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.19 , pp. 9627-9632
    • Holmgren, A.1
  • 61
    • 0021152329 scopus 로고
    • Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase
    • Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase. Hillson DA, Lambert N, Freedman RB, Methods Enzymol 1984 107 281 294
    • (1984) Methods Enzymol , vol.107 , pp. 281-294
    • Hillson, D.A.1    Lambert, N.2    Freedman, R.B.3


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