메뉴 건너뛰기




Volumn 1784, Issue 11, 2008, Pages 1601-1606

The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension

Author keywords

Antioxidant system; Cell surface; Fe containing enzyme; SOD; X ray structure

Indexed keywords

ANTIOXIDANT; ENZYME; IRON; MONOMER; SUPEROXIDE DISMUTASE;

EID: 54049115084     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.04.024     Document Type: Article
Times cited : (17)

References (39)
  • 3
    • 0028032403 scopus 로고
    • Escherichia coli expresses a copper- and zinc-containing superoxide dismutase
    • Benov L.T., and Fridovich I. Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J. Biol. Chem. 269 (1994) 25310-25314
    • (1994) J. Biol. Chem. , vol.269 , pp. 25310-25314
    • Benov, L.T.1    Fridovich, I.2
  • 7
    • 0035001195 scopus 로고    scopus 로고
    • Superoxide dismutase-deficient mutants of Helicobacter pylori are hypersensitive to oxidative stress and defective in host colonization
    • Seyler Jr. R.W., Olson J.W., and Maier R.J. Superoxide dismutase-deficient mutants of Helicobacter pylori are hypersensitive to oxidative stress and defective in host colonization. Infect. Immun. 69 (2001) 4034-4040
    • (2001) Infect. Immun. , vol.69 , pp. 4034-4040
    • Seyler Jr., R.W.1    Olson, J.W.2    Maier, R.J.3
  • 8
    • 0033013295 scopus 로고    scopus 로고
    • Generation of a superoxide dismutase (SOD)-deficient mutant of Campylobacter coli: evidence for the significance of SOD in Campylobacter survival and colonization
    • Purdy D., Cawthraw S., Dickinson J.H., Newell D.G., and Park S.F. Generation of a superoxide dismutase (SOD)-deficient mutant of Campylobacter coli: evidence for the significance of SOD in Campylobacter survival and colonization. Appl. Environ. Microbiol. 65 (1999) 2540-2546
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2540-2546
    • Purdy, D.1    Cawthraw, S.2    Dickinson, J.H.3    Newell, D.G.4    Park, S.F.5
  • 9
    • 0028933323 scopus 로고
    • Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus
    • Lah M.S., Dixon M.M., Pattridge K.A., Stallings W.C., Fee J.A., and Ludwig M.L. Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry 34 (1995) 1646-1660
    • (1995) Biochemistry , vol.34 , pp. 1646-1660
    • Lah, M.S.1    Dixon, M.M.2    Pattridge, K.A.3    Stallings, W.C.4    Fee, J.A.5    Ludwig, M.L.6
  • 11
    • 0025196784 scopus 로고
    • The 2.1Å-Ǻ resolution structure of iron superoxide dismutase from Pseudomonas ovalis
    • Stoddard B.L., Howell P.L., Ringe D., and Petsko G.A. The 2.1Å-Ǻ resolution structure of iron superoxide dismutase from Pseudomonas ovalis. Biochemistry 29 (1990) 8885-8893
    • (1990) Biochemistry , vol.29 , pp. 8885-8893
    • Stoddard, B.L.1    Howell, P.L.2    Ringe, D.3    Petsko, G.A.4
  • 12
    • 0027366226 scopus 로고
    • Purification of Helicobacter pylori superoxide dismutase and cloning and sequencing of the gene
    • Spiegelhalder C., Gerstenecker B., Kersten A., Schiltz E., and Kist M. Purification of Helicobacter pylori superoxide dismutase and cloning and sequencing of the gene. Infect. Immun. 61 (1993) 5315-5325
    • (1993) Infect. Immun. , vol.61 , pp. 5315-5325
    • Spiegelhalder, C.1    Gerstenecker, B.2    Kersten, A.3    Schiltz, E.4    Kist, M.5
  • 14
    • 0027653451 scopus 로고
    • In situ localization of the 60 k protein of Helicobacter pylori, which belongs to the family of heat shock proteins, by immuno-electron microscopy
    • Eschweiler B., Bohrmann B., Gerstenecker B., Schiltz E., and Kist M. In situ localization of the 60 k protein of Helicobacter pylori, which belongs to the family of heat shock proteins, by immuno-electron microscopy. Zentralbl. Bakteriol. 280 (1993) 73-85
    • (1993) Zentralbl. Bakteriol. , vol.280 , pp. 73-85
    • Eschweiler, B.1    Bohrmann, B.2    Gerstenecker, B.3    Schiltz, E.4    Kist, M.5
  • 15
    • 0030021824 scopus 로고    scopus 로고
    • Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis
    • Phadnis S.H., Parlow M.H., Levy M., Ilver D., Caulkins C.M., Connors J.B., and Dunn B.E. Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis. Infect. Immun. 64 (1996) 905-912
    • (1996) Infect. Immun. , vol.64 , pp. 905-912
    • Phadnis, S.H.1    Parlow, M.H.2    Levy, M.3    Ilver, D.4    Caulkins, C.M.5    Connors, J.B.6    Dunn, B.E.7
  • 16
    • 0037008715 scopus 로고    scopus 로고
    • Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis
    • Sabarth N., Lamer S., Zimny-Arndt U., Jungblut P.R., Meyer T.F., and Bumann D. Identification of surface proteins of Helicobacter pylori by selective biotinylation, affinity purification, and two-dimensional gel electrophoresis. J. Biol. Chem. 277 (2002) 27896-27902
    • (2002) J. Biol. Chem. , vol.277 , pp. 27896-27902
    • Sabarth, N.1    Lamer, S.2    Zimny-Arndt, U.3    Jungblut, P.R.4    Meyer, T.F.5    Bumann, D.6
  • 17
    • 17044389822 scopus 로고    scopus 로고
    • Subproteomes of soluble and structure-bound Helicobacter pylori proteins analyzed by two-dimensional gel electrophoresis and mass spectrometry
    • Backert, Kwok T., Schmid M., Selbach M., Moese S., Peek Jr. R.M., Konig W., Meyer T.F., and Jungblut P.R. Subproteomes of soluble and structure-bound Helicobacter pylori proteins analyzed by two-dimensional gel electrophoresis and mass spectrometry. Proteomics 5 (2005) 1331-1345
    • (2005) Proteomics , vol.5 , pp. 1331-1345
    • Backert1    Kwok, T.2    Schmid, M.3    Selbach, M.4    Moese, S.5    Peek Jr., R.M.6    Konig, W.7    Meyer, T.F.8    Jungblut, P.R.9
  • 18
    • 0031911053 scopus 로고    scopus 로고
    • Evidence for specific secretion rather than autolysis in the release of some Helicobacter pylori proteins
    • Vanet A., and Labigne A. Evidence for specific secretion rather than autolysis in the release of some Helicobacter pylori proteins. Infect. Immun. 66 (1998) 1023-1027
    • (1998) Infect. Immun. , vol.66 , pp. 1023-1027
    • Vanet, A.1    Labigne, A.2
  • 19
    • 0028236403 scopus 로고
    • Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni
    • Pesci E.C., Cottle D.L., and Pickett C.L. Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni. Infect. Immun. 62 (1994) 2687-2694
    • (1994) Infect. Immun. , vol.62 , pp. 2687-2694
    • Pesci, E.C.1    Cottle, D.L.2    Pickett, C.L.3
  • 20
    • 0002414103 scopus 로고
    • D.M., et al. (Ed), Oxford University Press, Oxford
    • Leslie A. In: D.M., et al. (Ed). Crystallographic Computing vol. V (1991), Oxford University Press, Oxford 50-61
    • (1991) Crystallographic Computing , vol.V , pp. 50-61
    • Leslie, A.1
  • 21
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • C.C.P.N. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
    • C.C.P.N. 41
  • 22
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 23
    • 84920325457 scopus 로고
    • AMoRe an automated package for molecular replacement
    • Navaza J. AMoRe an automated package for molecular replacement. Acta Crystallogr. A50 (1994) 157-163
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47 (1991) 110-119
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structure
    • Laskowski R.A., MacArthur M.W., Moss M.D., and Thorton J.M. PROCHECK: a program to check the stereochemical quality of protein structure. J. Appl. Crystallogr. 26 (1993) 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, M.D.3    Thorton, J.M.4
  • 27
    • 39749182759 scopus 로고    scopus 로고
    • Mn/Fe superoxide dismutase interaction fingerprints and prediction of oligomerization and metal cofactor from sequence
    • Wintjens R., Gilis D., and Rooman M. Mn/Fe superoxide dismutase interaction fingerprints and prediction of oligomerization and metal cofactor from sequence. Proteins 70 (2008) 1564-1577
    • (2008) Proteins , vol.70 , pp. 1564-1577
    • Wintjens, R.1    Gilis, D.2    Rooman, M.3
  • 28
    • 0035901552 scopus 로고    scopus 로고
    • Removing a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity
    • Edwards R.A., Whittaker M.M., Whittaker J.W., Baker E.N., and Jameson G.B. Removing a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity. Biochemistry 40 (2001) 4622-4632
    • (2001) Biochemistry , vol.40 , pp. 4622-4632
    • Edwards, R.A.1    Whittaker, M.M.2    Whittaker, J.W.3    Baker, E.N.4    Jameson, G.B.5
  • 29
    • 13244252222 scopus 로고    scopus 로고
    • The crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis
    • Munoz I.G., Moran J.F., Becana M., and Montoya G. The crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis. Protein Sci. 14 (2005) 387-394
    • (2005) Protein Sci. , vol.14 , pp. 387-394
    • Munoz, I.G.1    Moran, J.F.2    Becana, M.3    Montoya, G.4
  • 30
    • 0034598948 scopus 로고    scopus 로고
    • Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase
    • Borgstahl G.E., Pokross M., Chehab R., Sekher A., and Snell E.H. Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase. J. Mol. Biol. 296 (2000) 951-959
    • (2000) J. Mol. Biol. , vol.296 , pp. 951-959
    • Borgstahl, G.E.1    Pokross, M.2    Chehab, R.3    Sekher, A.4    Snell, E.H.5
  • 31
    • 0028938504 scopus 로고
    • X-ray absorption spectroscopy of the iron site in Escherichia coli Fe(III) superoxide dismutase
    • Tierney D.L., Fee J.A., Ludwig M.L., and Penner-Hahn J.E. X-ray absorption spectroscopy of the iron site in Escherichia coli Fe(III) superoxide dismutase. Biochemistry 34 (1995) 1661-1668
    • (1995) Biochemistry , vol.34 , pp. 1661-1668
    • Tierney, D.L.1    Fee, J.A.2    Ludwig, M.L.3    Penner-Hahn, J.E.4
  • 32
    • 0030888269 scopus 로고    scopus 로고
    • The conserved residue tyrosine 34 is essential for maximal activity of iron-superoxide dismutase from Escherichia coli
    • Hunter T., Ikebukuro K., Bannister W.H., Bannister J.V., and Hunter G.J. The conserved residue tyrosine 34 is essential for maximal activity of iron-superoxide dismutase from Escherichia coli. Biochemistry 36 (1997) 4925-4933
    • (1997) Biochemistry , vol.36 , pp. 4925-4933
    • Hunter, T.1    Ikebukuro, K.2    Bannister, W.H.3    Bannister, J.V.4    Hunter, G.J.5
  • 33
    • 0037051651 scopus 로고    scopus 로고
    • Second-sphere contributions to substrate-analogue binding in iron(III) superoxide dismutase
    • Xie J., Yikilmaz E., Miller A.F., and Brunold T.C. Second-sphere contributions to substrate-analogue binding in iron(III) superoxide dismutase. J. Am. Chem. Soc. 124 (2002) 3769-3774
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3769-3774
    • Xie, J.1    Yikilmaz, E.2    Miller, A.F.3    Brunold, T.C.4
  • 34
    • 31544448000 scopus 로고    scopus 로고
    • The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase
    • Yikilmaz E., Rodgers D.W., and Miller A.F. The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase. Biochemistry 45 (2006) 1151-1161
    • (2006) Biochemistry , vol.45 , pp. 1151-1161
    • Yikilmaz, E.1    Rodgers, D.W.2    Miller, A.F.3
  • 35
    • 37049007689 scopus 로고    scopus 로고
    • The cytoplasmic phosphoproteome of the Gram-negative bacterium Campylobacter jejuni: evidence for modification by unidentified protein kinases
    • Voisin S., Watson D.C., Tessier L., Ding W., Foote S., Bhatia S., Kelly J.F., and Young N.M. The cytoplasmic phosphoproteome of the Gram-negative bacterium Campylobacter jejuni: evidence for modification by unidentified protein kinases. Proteomics 7 (2007) 4338-4348
    • (2007) Proteomics , vol.7 , pp. 4338-4348
    • Voisin, S.1    Watson, D.C.2    Tessier, L.3    Ding, W.4    Foote, S.5    Bhatia, S.6    Kelly, J.F.7    Young, N.M.8
  • 36
    • 0026244229 scopus 로고
    • MOLSCRIPT:a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT:a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 37
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: photorealistic molecular graphics
    • Merritt E.A., and Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277 (1997) 505-524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 38
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and conturing of electron-density maps
    • Esnouf R.M. Further additions to MolScript version 1.4, including reading and conturing of electron-density maps. Acta Crystallogr. D 55 (1999) 938-940
    • (1999) Acta Crystallogr. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.