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Volumn 5, Issue 10, 1996, Pages 2125-2127

Crystallization and preliminary X-ray analysis of the monomeric Cu,Zn superoxide dismutase from Escherichia coli

Author keywords

crystals; enzyme structure; Escherichia coli; metal proteins; monomer dimer equilibrium

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE;

EID: 0029910087     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051020     Document Type: Article
Times cited : (9)

References (25)
  • 1
    • 0029608758 scopus 로고
    • Synthesis and characterization of a monomeric mutant Cu/Zn superoxide dismutase with partially reconstituted enzymic activity
    • Banci L, Bertini I, Chiu CY, Mullenbach GT, Viezzoli MS. 1995. Synthesis and characterization of a monomeric mutant Cu/Zn superoxide dismutase with partially reconstituted enzymic activity. Eur J Biochem 234:855-860.
    • (1995) Eur J Biochem , vol.234 , pp. 855-860
    • Banci, L.1    Bertini, I.2    Chiu, C.Y.3    Mullenbach, G.T.4    Viezzoli, M.S.5
  • 2
    • 0023463279 scopus 로고
    • Aspects of the structure, function and application of superoxide dismutase
    • Bannister JV, Bannister WH, Rotilio G. 1987. Aspects of the structure, function and application of superoxide dismutase. CRC Crit Rev Biochem 22:111-180.
    • (1987) CRC Crit Rev Biochem , vol.22 , pp. 111-180
    • Bannister, J.V.1    Bannister, W.H.2    Rotilio, G.3
  • 3
    • 0028841185 scopus 로고
    • Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli
    • Battistoni A, Rotilio G. 1995. Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli. FEBS Lett 374:199-202.
    • (1995) FEBS Lett , vol.374 , pp. 199-202
    • Battistoni, A.1    Rotilio, G.2
  • 4
    • 0028228085 scopus 로고
    • Conserved patterns in superoxide dismutase structure
    • Bordo D, Djinovic-Carugo K, Bolognesi M. 1994. Conserved patterns in superoxide dismutase structure. J Mol Biol 238:366-368.
    • (1994) J Mol Biol , vol.238 , pp. 366-368
    • Bordo, D.1    Djinovic-Carugo, K.2    Bolognesi, M.3
  • 5
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4. The CCP4 suite: Programs for protein crystallography
    • CCP4. 1994. Collaborative Computational Project Number 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50:760-767.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-767
  • 7
    • 0026586029 scopus 로고
    • Evolutionary conservativeness of electric field in the Cu,Zn superoxide dismutase active site
    • Desideri A, Falconi M, Polticelli F, Bolognesi M, Djinovic K, Rotilio G. 1992. Evolutionary conservativeness of electric field in the Cu,Zn superoxide dismutase active site. J Mol Biol 223:337-342.
    • (1992) J Mol Biol , vol.223 , pp. 337-342
    • Desideri, A.1    Falconi, M.2    Polticelli, F.3    Bolognesi, M.4    Djinovic, K.5    Rotilio, G.6
  • 8
    • 0021760092 scopus 로고
    • Comprehensive set of sequence analysis programs for the VAX
    • Devereux J, Haberli P, Smithies OA. 1984. Comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12:387-395.
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haberli, P.2    Smithies, O.A.3
  • 9
    • 0026735131 scopus 로고
    • Crystal structure solution and refinement of the semi-synthetic cobalt-substituted bovine erythrocyte superoxide dismutase at 2 Å resolution
    • Djinovic K, Coda A, Antolini L, Pelosi G, Desideri A, Falconi M, Rotilio G, Bolognesi M. 1992a. Crystal structure solution and refinement of the semi-synthetic cobalt-substituted bovine erythrocyte superoxide dismutase at 2 Å resolution. J Mol Biol 226:227-238.
    • (1992) J Mol Biol , vol.226 , pp. 227-238
    • Djinovic, K.1    Coda, A.2    Antolini, L.3    Pelosi, G.4    Desideri, A.5    Falconi, M.6    Rotilio, G.7    Bolognesi, M.8
  • 13
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom HR, Griffiths AD, Johnson KS, Chiswell DJ, Hudson P, Winter G. 1991. Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res 19:4133-4137.
    • (1991) Nucleic Acids Res , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 15
    • 0029294031 scopus 로고
    • Subunit interaction enhances enzyme activity and stability of sweet potato cytosolic Cu,Zn superoxide dismutase purified by a His-tagged recombinant protein method
    • Lin CT, Lin MT, Chen YT, Shaw JF. 1995. Subunit interaction enhances enzyme activity and stability of sweet potato cytosolic Cu,Zn superoxide dismutase purified by a His-tagged recombinant protein method. Plant Mol Biol 25:303-311.
    • (1995) Plant Mol Biol , vol.25 , pp. 303-311
    • Lin, C.T.1    Lin, M.T.2    Chen, Y.T.3    Shaw, J.F.4
  • 16
    • 0018789696 scopus 로고
    • Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents
    • Malinowski DP, Fridovich I. 1979. Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents. Biochemistry 18:5055-5060.
    • (1979) Biochemistry , vol.18 , pp. 5055-5060
    • Malinowski, D.P.1    Fridovich, I.2
  • 17
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. 1968. Solvent content of protein crystals. J Mol Biol 33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 18
    • 0011448278 scopus 로고
    • Filamentous coliphage M13 as a cloning vehicle: Insertion of a Hind III fragment of the lac regulatory region in M13 replicative form in vitro
    • Messing J, Gronenborg B, Mueller-Hill B, Hofschneider PH. 1977. Filamentous coliphage M13 as a cloning vehicle: Insertion of a Hind III fragment of the lac regulatory region in M13 replicative form in vitro. Proc Natl Acad Sci USA 74:3642-3646.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 3642-3646
    • Messing, J.1    Gronenborg, B.2    Mueller-Hill, B.3    Hofschneider, P.H.4
  • 19
    • 0026711256 scopus 로고
    • Atomic structures of wild type and thermostable mutant recombinant human Cu,Zn superoxide dismutase
    • Parge HE, Hallewell RA, Tainer JA. 1992. Atomic structures of wild type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proc Natl Acad Sci USA 89:6109-6113.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6109-6113
    • Parge, H.E.1    Hallewell, R.A.2    Tainer, J.A.3
  • 20
    • 0016207797 scopus 로고
    • Isolation of a new copper and zinc superoxide dismutase. Bacteriocuprein
    • Puget K, Michelson AM. 1974. Isolation of a new copper and zinc superoxide dismutase. Bacteriocuprein. Biochem Biophys Res Commun 55:830-838.
    • (1974) Biochem Biophys Res Commun , vol.55 , pp. 830-838
    • Puget, K.1    Michelson, A.M.2
  • 21
    • 0017811466 scopus 로고
    • On the quaternary structure of copper-zinc superoxide dismutases. Reversible dissociation into protomers of the isozyme I from wheat germ
    • Rigo A, Marmocchi F, Cocco D, Viglino P, Rotilio G. 1978. On the quaternary structure of copper-zinc superoxide dismutases. Reversible dissociation into protomers of the isozyme I from wheat germ. Biochemistry 175:534-537.
    • (1978) Biochemistry , vol.175 , pp. 534-537
    • Rigo, A.1    Marmocchi, F.2    Cocco, D.3    Viglino, P.4    Rotilio, G.5
  • 24
    • 0025339960 scopus 로고
    • Copper-zinc superoxide dismutase of Caulobacter crescentus: Cloning, sequencing and mapping of the gene and periplasmic location of the enzyme
    • Steinman HM, Ely B. 1990. Copper-zinc superoxide dismutase of Caulobacter crescentus: Cloning, sequencing and mapping of the gene and periplasmic location of the enzyme. J Bacteriol 172:2901-2910.
    • (1990) J Bacteriol , vol.172 , pp. 2901-2910
    • Steinman, H.M.1    Ely, B.2
  • 25
    • 0020374498 scopus 로고
    • Determination and analysis of the 2 Å structure of bovine copper,zinc superoxide dismutase
    • Tainer JA, Getzoff ED, Beem KM, Richardson JS, Richardson DC. 1982. Determination and analysis of the 2 Å structure of bovine copper,zinc superoxide dismutase. J Mol Biol 160:287-303.
    • (1982) J Mol Biol , vol.160 , pp. 287-303
    • Tainer, J.A.1    Getzoff, E.D.2    Beem, K.M.3    Richardson, J.S.4    Richardson, D.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.