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Volumn 5, Issue 4, 1998, Pages 310-316

Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 Å resolution

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBATE OXIDASE; LACCASE; OXIDOREDUCTASE;

EID: 0031979620     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0498-310     Document Type: Article
Times cited : (353)

References (42)
  • 1
    • 0030025889 scopus 로고    scopus 로고
    • A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability
    • Xu, F. et al. A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability. Biochim. Biophysica Acta 1292, 303-311 (1996).
    • (1996) Biochim. Biophysica Acta , vol.1292 , pp. 303-311
    • Xu, F.1
  • 2
    • 0029937108 scopus 로고    scopus 로고
    • Oxidation of phenols, anilines and benzenethiols by fungal laccases: Correlation between activity and redox potentials as well as halide inhibition
    • Xu, F. Oxidation of phenols, anilines and benzenethiols by fungal laccases: correlation between activity and redox potentials as well as halide inhibition. Biochemistry 35, 7608-7614 (1996).
    • (1996) Biochemistry , vol.35 , pp. 7608-7614
    • Xu, F.1
  • 3
    • 0027240897 scopus 로고
    • A laccase associated with lignification in loblolly pine xylem
    • Bao, W., O'Malley, D.M., Whetten, R. & Sederoff, R.R. A laccase associated with lignification in loblolly pine xylem. Science 260, 672-674 (1993).
    • (1993) Science , vol.260 , pp. 672-674
    • Bao, W.1    O'Malley, D.M.2    Whetten, R.3    Sederoff, R.R.4
  • 4
    • 0001835041 scopus 로고
    • The importance of phenol oxidase activity in lignin degradation by the white rot fungus Sporotrichum pulverulentum
    • Ander, P. & Eriksson, K.E. The importance of phenol oxidase activity in lignin degradation by the white rot fungus Sporotrichum pulverulentum. Arch. Microbiol. 109, 1-8 (1976).
    • (1976) Arch. Microbiol. , vol.109 , pp. 1-8
    • Ander, P.1    Eriksson, K.E.2
  • 5
    • 0025341273 scopus 로고
    • Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes
    • Kersten, P.J., Kalyanaraman, B., Hammel, K.E., Reinhammar, B. & Kirk, T.K. Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes. Biochem. J. 268, 475-480 (1990).
    • (1990) Biochem. J. , vol.268 , pp. 475-480
    • Kersten, P.J.1    Kalyanaraman, B.2    Hammel, K.E.3    Reinhammar, B.4    Kirk, T.K.5
  • 6
    • 0001320226 scopus 로고
    • Studies on the laccase of Lentinus edodes: Specificity, localization and assocition with the development of fruiting bodies
    • Leatham, G.F. & Stahmann, M.A. Studies on the laccase of Lentinus edodes: specificity, localization and assocition with the development of fruiting bodies. J. Gen. Microbiol. 125, 147-157 (1981).
    • (1981) J. Gen. Microbiol. , vol.125 , pp. 147-157
    • Leatham, G.F.1    Stahmann, M.A.2
  • 7
    • 0002964288 scopus 로고    scopus 로고
    • Copper metalloenzymes
    • (ed. Sinnott, M.) Academic Press, London
    • Messerschmidt, A. Copper metalloenzymes. In Comprehensive Biological Catalysis Vol. III (ed. Sinnott, M.) 401-426 (Academic Press, London, 1997).
    • (1997) Comprehensive Biological Catalysis , vol.3 , pp. 401-426
    • Messerschmidt, A.1
  • 9
    • 77956895783 scopus 로고
    • Copper-containing oxidases and superoxide dismutase
    • (ed. Boyer, P.) Academic Press, New York
    • Malmström, B.G., Andréasson, L.E. & Reinhammar, R. Copper-containing oxidases and superoxide dismutase. In The Enzymes Vol. 12 (ed. Boyer, P.) 507-578 (Academic Press, New York, 1975).
    • (1975) The Enzymes , vol.12 , pp. 507-578
    • Malmström, B.G.1    Andréasson, L.E.2    Reinhammar, R.3
  • 10
    • 0026411154 scopus 로고
    • Copper protein structures
    • Adman, E.T. Copper protein structures. Adv. Protein Chem. 42, 145-197 (1991).
    • (1991) Adv. Protein Chem. , vol.42 , pp. 145-197
    • Adman, E.T.1
  • 11
    • 0026603624 scopus 로고
    • Refined crystal structure of ascorbate oxidase at 1.9Å resolution
    • Messerschmidt, A. et al. Refined crystal structure of ascorbate oxidase at 1.9Å resolution. J. Mol. Biol. 224, 179-205 (1992).
    • (1992) J. Mol. Biol. , vol.224 , pp. 179-205
    • Messerschmidt, A.1
  • 12
    • 3042958993 scopus 로고    scopus 로고
    • The X-ray structure of human serum ceruloplasmin at 3.1Å: Nature of the copper centres
    • Zaitseva, I. et al. The X-ray structure of human serum ceruloplasmin at 3.1Å: nature of the copper centres. J. Biol. Inorg. Chem. 1, 15-23 (1996).
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 15-23
    • Zaitseva, I.1
  • 13
    • 0011509370 scopus 로고    scopus 로고
    • Structural and functional aspects of metal sites in biology
    • Holm, R.H., Kennepohl, P. & Solomon, E.I. Structural and functional aspects of metal sites in biology. Chem Rev 96, 2239-2314 (1996).
    • (1996) Chem Rev , vol.96 , pp. 2239-2314
    • Holm, R.H.1    Kennepohl, P.2    Solomon, E.I.3
  • 14
    • 0024293340 scopus 로고
    • Structure of Azurin from Alcaligenes denitrificans Refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules
    • Baker, E.N. Structure of Azurin from Alcaligenes denitrificans Refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules. J. Mol. Biol. 203, 1071-1095 (1988).
    • (1988) J. Mol. Biol. , vol.203 , pp. 1071-1095
    • Baker, E.N.1
  • 15
    • 0025249905 scopus 로고
    • Crystal structure of plastocyanin from a green alga, Enteromorpha prolifera
    • Collyer, C.A., Guss, J.M., Sugimura, Y., Yoshizaki, F. & Freeman, H.C. Crystal structure of plastocyanin from a green alga, Enteromorpha prolifera. J. Mol. Biol. 211, 617-632 (1990).
    • (1990) J. Mol. Biol. , vol.211 , pp. 617-632
    • Collyer, C.A.1    Guss, J.M.2    Sugimura, Y.3    Yoshizaki, F.4    Freeman, H.C.5
  • 16
    • 0030975668 scopus 로고    scopus 로고
    • Structural comparison of cupredoxin domains: Domain recycling to construct proteins with novel functions
    • Murphy, M.E.P., Lindley, P.F. & Adman, E.T. Structural comparison of cupredoxin domains: domain recycling to construct proteins with novel functions. Protein Sci. 6, 761-770 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 761-770
    • Murphy, M.E.P.1    Lindley, P.F.2    Adman, E.T.3
  • 17
    • 0001886633 scopus 로고
    • Laccase
    • (ed. Lontie, R.) CRC Press, Boca Raton, Florida
    • Reinhammar, B. Laccase. In Copper Proteins and Copper Enzymes Vol. 3 (ed. Lontie, R.) 1-36 (CRC Press, Boca Raton, Florida, 1984).
    • (1984) Copper Proteins and Copper Enzymes , vol.3 , pp. 1-36
    • Reinhammar, B.1
  • 19
    • 0025058305 scopus 로고
    • The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin: Modelling and structural relationships
    • Messerschmidt, A. & Huber, R. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin: modelling and structural relationships. Eur. J. Biochem. 187, 341-352 (1990).
    • (1990) Eur. J. Biochem. , vol.187 , pp. 341-352
    • Messerschmidt, A.1    Huber, R.2
  • 20
    • 0001814457 scopus 로고
    • Rack-induced bonding in blue copper proteins: Spectroscopic properties and reduction potential of azurin mutant Met-121 -> Leu
    • Karlsson, B.G., Aasa, R., Malmström, B.G. & Lundberg, L.G. Rack-induced bonding in blue copper proteins: spectroscopic properties and reduction potential of azurin mutant Met-121 -> Leu. FEBS Lett. 253, 99-102 (1989).
    • (1989) FEBS Lett. , vol.253 , pp. 99-102
    • Karlsson, B.G.1    Aasa, R.2    Malmström, B.G.3    Lundberg, L.G.4
  • 21
    • 0029274711 scopus 로고
    • Electronic structure of the reduced blue copper active site: Contributions to reduction potentials and geometry
    • Guckert, J.A., Lowry, M.D. & Solomon, E.I. Electronic structure of the reduced blue copper active site: contributions to reduction potentials and geometry. J. Am. Chem. Soc. 117, 2817-2844 (1995).
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2817-2844
    • Guckert, J.A.1    Lowry, M.D.2    Solomon, E.I.3
  • 22
    • 0026646297 scopus 로고
    • X-ray crystallographic characterisation of type-2-depleted ascorbate oxidase from zucchini
    • Messerschmidt, A., Steigemann, W., Huber, R., Lang, G. & Kroneck, P.M.H. X-ray crystallographic characterisation of type-2-depleted ascorbate oxidase from zucchini. Eur. J. Biochem 209, 179-205 (1992).
    • (1992) Eur. J. Biochem , vol.209 , pp. 179-205
    • Messerschmidt, A.1    Steigemann, W.2    Huber, R.3    Lang, G.4    Kroneck, P.M.H.5
  • 23
    • 0000485692 scopus 로고
    • Chemical and Spectroscopic proerties of the binuclear copper active site in Rhus laccase: Direct conformation of a reduced binuclear Type 3 copper site in type 2 depleted laccase and intramolecular coupling of the type 3 to the type 1 and type 2 copper sites
    • LuBien, C.D. et al. Chemical and Spectroscopic proerties of the binuclear copper active site in Rhus laccase: direct conformation of a reduced binuclear Type 3 copper site in type 2 depleted laccase and intramolecular coupling of the type 3 to the type 1 and type 2 copper sites. J. Am. Chem. Soc. 103, 7014-7016 (1981).
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 7014-7016
    • LuBien, C.D.1
  • 24
    • 0002338540 scopus 로고    scopus 로고
    • Spectroscopy of multi-copper oxidases
    • (ed. Messerschmidt, A.) World Scientific, Singapore
    • Solomon, E.I., Machonkin, T.E. & Sundaram, U.M. Spectroscopy of multi-copper oxidases. in Multi-copper oxidases (ed. Messerschmidt, A.) 103-127 (World Scientific, Singapore, 1997).
    • (1997) Multi-copper Oxidases , pp. 103-127
    • Solomon, E.I.1    Machonkin, T.E.2    Sundaram, U.M.3
  • 25
    • 33845283452 scopus 로고
    • X-ray absorption edge determination of the oxidation state and coordination number of copper: Application to the type 3 site in Rhus vernicifera laccase and its reaction with oxygen
    • Kau, L.-S., Spira-Solomon, D.J., Penner-Hahn, J.E., Hodgson, K.O. & Solomon, E.I. X-ray absorption edge determination of the oxidation state and coordination number of copper: application to the type 3 site in Rhus vernicifera laccase and its reaction with oxygen. J. Am. Chem. Soc. 109, 6433-6442 (1987).
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6433-6442
    • Kau, L.-S.1    Spira-Solomon, D.J.2    Penner-Hahn, J.E.3    Hodgson, K.O.4    Solomon, E.I.5
  • 26
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Thurston, C.F. The structure and function of fungal laccases. Microbiology 140, 19-26 (1994).
    • (1994) Microbiology , vol.140 , pp. 19-26
    • Thurston, C.F.1
  • 27
    • 0027914978 scopus 로고
    • Electronic structure contributions to function in bioinorganic chemistry
    • Solomon, E.I. & Lowery, M.D. Electronic structure contributions to function in bioinorganic chemistry. Science 259, 1575-1581 (1993).
    • (1993) Science , vol.259 , pp. 1575-1581
    • Solomon, E.I.1    Lowery, M.D.2
  • 29
    • 0017152398 scopus 로고
    • Selective removal of type 2 copper from Rhus vernicifera laccase
    • Graziani, M.T., Morpurgo, L., Rotilio, G. & Mondovi, B. Selective removal of type 2 copper from Rhus vernicifera laccase. FEBS Lett. 70, 87-(1976).
    • (1976) FEBS Lett. , vol.70 , pp. 87
    • Graziani, M.T.1    Morpurgo, L.2    Rotilio, G.3    Mondovi, B.4
  • 30
    • 0002421841 scopus 로고    scopus 로고
    • Bioinorganic chemistry of laccase
    • (ed. Messerschmidt, A.) World Scientific, Singapore
    • McMillin, D.R. & Eggleston, M.K. Bioinorganic chemistry of laccase. in Multi-copper oxidases (ed. Messerschmidt, A.) 129-166 (World Scientific, Singapore, 1997).
    • (1997) Multi-copper Oxidases , pp. 129-166
    • McMillin, D.R.1    Eggleston, M.K.2
  • 31
    • 0018526048 scopus 로고
    • Spectroscopic and catalytic properties of Rhus vernicifera laccase depleted in type 2 copper
    • Reinhammar, B. & Oda, Y. Spectroscopic and catalytic properties of Rhus vernicifera laccase depleted in type 2 copper. J. Inorg. Biochem. 11, 115-127 (1979).
    • (1979) J. Inorg. Biochem. , vol.11 , pp. 115-127
    • Reinhammar, B.1    Oda, Y.2
  • 32
    • 9844267975 scopus 로고    scopus 로고
    • Crystallisation and preliminary X-ray analysis of the laccase from Coprinus cinereus
    • Ducros, V. et al. Crystallisation and preliminary X-ray analysis of the laccase from Coprinus cinereus. Acta. Crystallogr. D 53, 605-607 (1997).
    • (1997) Acta. Crystallogr. , vol.53 D , pp. 605-607
    • Ducros, V.1
  • 33
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • (eds Sawyer, L., Issacs, N. & Bailey, S.) Science and Engineering Research Council, Daresbury, U.K
    • Otwinowski, Z. Oscillation data reduction program. In Data collection and Processing: proceedings of the CCP4 study weekend (eds Sawyer, L., Issacs, N. & Bailey, S.) 56-62 (Science and Engineering Research Council, Daresbury, U.K, 1993).
    • (1993) Data Collection and Processing: Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 34
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 35
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50, 157-163 (1994).
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 36
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum likelihood method
    • Murshudov, G.N., Vagin, A.A. & Dodson, E.J. Refinement of macromolecular structures by the maximum likelihood method. Acta Crystallogr D 53, 240-255 (1997).
    • (1997) Acta Crystallogr , vol.53 D , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 37
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475 (1992).
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 38
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. & Wilson, K.S. Automated refinement of protein models. Acta Crystallogr. D49, 129-147 (1993).
    • (1993) Acta Crystallogr. , vol.D49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 39
    • 79952608525 scopus 로고
    • Accurate bond length and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. Accurate bond length and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A 47, 392-400 (1991).
    • (1991) Acta Crystallogr. , vol.47 A , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 41
    • 0017411710 scopus 로고
    • The protein data bank: A computer-based archival file for macromolecular structures
    • Bernstein, F.C. et al. The protein data bank: a computer-based archival file for macromolecular structures. J. Mol. Biol 112, 535-542 (1977).
    • (1977) J. Mol. Biol , vol.112 , pp. 535-542
    • Bernstein, F.C.1
  • 42
    • 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, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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