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Volumn 278, Issue 13, 2011, Pages 2283-2295

Crystal structure of an ascomycete fungal laccase from Thielavia arenaria - Common structural features of asco-laccases

Author keywords

ascomycete; C terminal plug; laccase; proton transfer; redox potential

Indexed keywords

AMINO ACID; CHLORIDE; COPPER; HOMODIMER; LACCASE;

EID: 80051483501     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08146.x     Document Type: Article
Times cited : (64)

References (63)
  • 1
    • 0026603624 scopus 로고
    • Refined crystal structure of ascorbate oxidase at 1.9 Å resolution
    • Messerschmidt A, Ladenstein R, &, Huber R, (1992) Refined crystal structure of ascorbate oxidase at 1.9 Å resolution. J Mol Biol 224, 179-205.
    • (1992) J Mol Biol , vol.224 , pp. 179-205
    • Messerschmidt, A.1    Ladenstein, R.2    Huber, R.3
  • 5
    • 33645659250 scopus 로고    scopus 로고
    • Structure of phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center
    • Smith AW, Camara-Artigas A, Wang M, Allen JP, &, Francisco WA, (2006) Structure of phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center. Biochemistry 45, 4378-4387.
    • (2006) Biochemistry , vol.45 , pp. 4378-4387
    • Smith, A.W.1    Camara-Artigas, A.2    Wang, M.3    Allen, J.P.4    Francisco, W.A.5
  • 6
    • 0001329209 scopus 로고    scopus 로고
    • Cyclic voltammetry and electrocatalysis of the blue copper oxidase Polyporus versicolor laccase
    • Thuesen MH, Farver O, Reinhammar B, &, Ulstrup J, (1998) Cyclic voltammetry and electrocatalysis of the blue copper oxidase Polyporus versicolor laccase. Acta Chem Scand 52, 555-562. (Pubitemid 128551444)
    • (1998) Acta Chemica Scandinavica , vol.52 , Issue.5 , pp. 555-562
    • Thuesen, M.H.1    Farver, O.2    Reinhammar, B.3    Ulstrup, J.4
  • 7
    • 34247538548 scopus 로고    scopus 로고
    • 2 reduction based on rational attachment of a blue copper oxidase to a graphite surface
    • DOI 10.1039/b703114a
    • 2 reduction based on rational attachment of a blue copper oxidase to a graphite surface. Chem Commun 17, 1710-1712. (Pubitemid 46652256)
    • (2007) Chemical Communications , Issue.17 , pp. 1710-1712
    • Blanford, C.F.1    Heath, R.S.2    Armstrong, F.A.3
  • 8
    • 29044440810 scopus 로고    scopus 로고
    • Applications of oxidoreductases: Recent progress
    • Xu F, (2005) Applications of oxidoreductases: recent progress. Ind Biotechnol 1, 38-50.
    • (2005) Ind Biotechnol , vol.1 , pp. 38-50
    • Xu, F.1
  • 9
    • 33746142419 scopus 로고    scopus 로고
    • Industrial and biotechnological applications of laccases: A review
    • DOI 10.1016/j.biotechadv.2006.04.003, PII S0734975006000619
    • Rodríguez Couto S, &, Toca Herrera JL, (2006) Industrial and biotechnological applications of laccases: a review. Biotechnol Adv 24, 500-513. (Pubitemid 44082015)
    • (2006) Biotechnology Advances , vol.24 , Issue.5 , pp. 500-513
    • Rodriguez Couto, S.1    Toca Herrera, J.L.2
  • 11
    • 0037062591 scopus 로고    scopus 로고
    • Crystal structure of a four-copper laccase complexed with an arylamine: Insights into substrate recognition and correlation with kinetics
    • DOI 10.1021/bi0201318
    • Bertrand T, Jolivalt C, Briozzo P, Caminade E, Joly N, Madzak C, &, Mougin C, (2002) Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics. Biochemistry 41, 7325-7333. (Pubitemid 34602449)
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7325-7333
    • Bertrand, T.1    Jolivalt, C.2    Briozzo, P.3    Caminade, E.4    Joly, N.5    Madzak, C.6    Mougin, C.7
  • 12
    • 0037020063 scopus 로고    scopus 로고
    • Crystal structure of a laccase from the fungus Trameters versicolor at 1.90 Å resolution containing a full complement of coppers
    • Piontek K, Antorini M, &, Choinowski T, (2002) Crystal structure of a laccase from the fungus Trameters versicolor at 1.90 Å resolution containing a full complement of coppers. J Biol Chem 277, 37663-37669.
    • (2002) J Biol Chem , vol.277 , pp. 37663-37669
    • Piontek, K.1    Antorini, M.2    Choinowski, T.3
  • 13
    • 4444352552 scopus 로고    scopus 로고
    • The structure of Rigidoporus lignosus laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair
    • DOI 10.1016/j.jmb.2004.07.100, PII S0022283604009544
    • Garavaglia S, Cambria MT, Miglio M, Ragusa S, Iacobazzi V, Palmieri F, D'Ambrosio C, Scaloni A, &, Rizzi M, (2004) The structure of Rigidoporus lignosus laccase containing a full complement of copper ions, reveals an asymmetrical arrangement for the T3 copper pair. J Mol Biol 342, 1519-1531. (Pubitemid 39208675)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.5 , pp. 1519-1531
    • Garavaglia, S.1    Teresa Cambria, M.2    Miglio, M.3    Ragusa, S.4    Iacobazzi, V.5    Palmieri, F.6    D'Ambrosio, C.7    Scaloni, A.8    Rizzi, M.9
  • 16
    • 35948977727 scopus 로고    scopus 로고
    • Crystal structure of a blue laccase from Lentinus tigrinus: Evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases
    • doi.
    • Ferraroni M, Myasoedova NM, Schmatchenko V, Leontievsky AA, Golovleva LA, Scozzafava A, &, Briganti F, (2007) Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases. BMC Struct Biol 7, 60, doi:.
    • (2007) BMC Struct Biol , vol.7 , pp. 60
    • Ferraroni, M.1    Myasoedova, N.M.2    Schmatchenko, V.3    Leontievsky, A.A.4    Golovleva, L.A.5    Scozzafava, A.6    Briganti, F.7
  • 17
    • 49549095554 scopus 로고    scopus 로고
    • Crystal structure of the blue multicopper oxidase from the whiterot fungus Trametes trogii complexed with p-toluate
    • Matera I, Gullotto A, Tilli S, Ferraroni M, Scozzafava A, &, Briganti F, (2008) Crystal structure of the blue multicopper oxidase from the whiterot fungus Trametes trogii complexed with p-toluate. Inorg Chim Acta 361, 4129-4137.
    • (2008) Inorg Chim Acta , vol.361 , pp. 4129-4137
    • Matera, I.1    Gullotto, A.2    Tilli, S.3    Ferraroni, M.4    Scozzafava, A.5    Briganti, F.6
  • 19
    • 80955177229 scopus 로고    scopus 로고
    • Reference withdrawn
    • Reference withdrawn
  • 22
    • 62849083557 scopus 로고    scopus 로고
    • X-ray structure of a two-domain type laccase: A missing link in the evolution of multi-copper proteins
    • Komori H, Miyazaki K, &, Higuchi Y, (2009) X-ray structure of a two-domain type laccase: a missing link in the evolution of multi-copper proteins. FEBS Lett 583, 1189-1195.
    • (2009) FEBS Lett , vol.583 , pp. 1189-1195
    • Komori, H.1    Miyazaki, K.2    Higuchi, Y.3
  • 23
    • 65649097276 scopus 로고    scopus 로고
    • Crystal structure of a two-domain multicopper oxidase: Implications for the evolution of multicopper blue proteins
    • Lawton TJ, Sayavedra-Soto LA, Arp DJ, &, Rosenzweig AC, (2009) Crystal structure of a two-domain multicopper oxidase: implications for the evolution of multicopper blue proteins. J Biol Chem 284, 10174-10180.
    • (2009) J Biol Chem , vol.284 , pp. 10174-10180
    • Lawton, T.J.1    Sayavedra-Soto, L.A.2    Arp, D.J.3    Rosenzweig, A.C.4
  • 27
    • 0035905357 scopus 로고    scopus 로고
    • Oxygen binding, activation, and reduction to water by copper proteins
    • DOI 10.1002/1521-3773(20011217)40:24<4570::AID-ANIE4570>3.0.CO;2-4
    • Solomon EI, Chen P, Metz M, Lee S-K, &, Palmer AE, (2001) Oxygen binding, activation, and reduction to water by copper enzymes. Angew Chem Int Ed 40, 4570-4590. (Pubitemid 34032186)
    • (2001) Angewandte Chemie - International Edition , vol.40 , Issue.24 , pp. 4570-4590
    • Solomon, E.I.1    Chen, P.2    Metz, M.3    Lee, S.-K.4    Palmer, A.E.5
  • 28
    • 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
    • DOI 10.1021/bi952971a
    • Xu F, (1996) Oxidation of phenols, anilines, and benzenethiols by fungal laccases: correlation between activity and redox potentials as well as halide inhibition. Biochemistry 35, 7608-7614. (Pubitemid 26189831)
    • (1996) Biochemistry , vol.35 , Issue.23 , pp. 7608-7614
    • Xu, F.1
  • 29
    • 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
    • DOI 10.1016/0167-4838(95)00210-3
    • Xu F, Shin W, Brown SH, Wahleithner JA, Sundaram UM, &, Solomon EI, (1996) A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability. Biochim Biophys Acta Protein Struct Mol Enzymol 1292, 303-311. (Pubitemid 26071166)
    • (1996) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1292 , Issue.2 , pp. 303-311
    • Xu, F.1    Shin, W.2    Brown, S.H.3    Wahleithner, J.A.4    Sundaram, U.M.5    Solomon, E.I.6
  • 31
    • 0034819344 scopus 로고    scopus 로고
    • Enzymatic and electrochemical oxidation of N-hydroxy compounds: Redox potential, electron-transfer kinetics, and radical stability
    • DOI 10.1046/j.1432-1327.2001.02328.x
    • Xu F, Deussen HW, Lopez B, Lam L, &, Li K, (2001) Enzymatic and electrochemical oxidation of N-hydroxy compounds: redox potential, electron transfer kinetics, and radical stability. Eur J Biochem 268, 4169-4176. (Pubitemid 32862877)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.15 , pp. 4169-4176
    • Xu, F.1    Deussen, H.-J.W.2    Lopez, B.3    Lam, L.4    Li, K.5
  • 35
    • 17644363018 scopus 로고    scopus 로고
    • Role of aspartate 94 in the decay of the peroxide intermediate in the multicopper oxidase Fet3p
    • DOI 10.1021/bi047379c
    • Quintanar L, Stoj C, Wang T-P, Kosman DJ, &, Solomon EI, (2005) Role of aspartate 94 in the decay of the peroxide intermediate in the multicopper oxidase Fet3p. Biochemistry 44, 6081-6091. (Pubitemid 40570702)
    • (2005) Biochemistry , vol.44 , Issue.16 , pp. 6081-6091
    • Quintanar, L.1    Stoj, C.2    Wang, T.-P.3    Kosman, D.J.4    Solomon, E.I.5
  • 36
    • 0346500440 scopus 로고    scopus 로고
    • Molecular Cloning and Expression in Saccharomyces cerevisiae of Laccase Gene from the Ascomycete Melanocarpus albomyces
    • DOI 10.1128/AEM.70.1.137-144.2004
    • Kiiskinen L-L, &, Saloheimo M, (2004) Molecular cloning and expression in Saccharomyces cerevisiae of a laccase gene from the ascomycete Melanocarpus albomyces. Appl Environ Microbiol 70, 137-144. (Pubitemid 38090197)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.1 , pp. 137-144
    • Kiiskinen, L.-L.1    Saloheimo, M.2
  • 37
    • 0023838115 scopus 로고
    • Characterization of two allelic forms of Neurospora crassa laccase. Amino- and carboxyl-terminal processing of a precursor
    • Germann U, Muller G, Hunziker P, &, Lerch K, (1988) Characterization of two allelic forms of Neurospora crassa laccase. Amino- and carboxyl-terminal processing of a precursor. J Biol Chem 263, 885-896. (Pubitemid 18044718)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.2 , pp. 885-896
    • Germann, U.A.1    Muller, G.2    Hunziker, P.E.3    Lerch, K.4
  • 38
    • 10244222256 scopus 로고    scopus 로고
    • Isolation and characterization of a laccase gene from Podospora anserina
    • Fernandez-Larrea J, &, Stahl U, (1996) Isolation and characterization of a laccase gene from Podospora anserina. Mol Gen Genet 252, 539-551.
    • (1996) Mol Gen Genet , vol.252 , pp. 539-551
    • Fernandez-Larrea, J.1    Stahl, U.2
  • 40
    • 70349950471 scopus 로고    scopus 로고
    • Essential role of the C-terminus in Melanocarpus albomyces laccase for enzyme production, catalytic properties and structure
    • Andberg M, Hakulinen N, Auer S, Saloheimo M, Koivula A, Rouvinen J, &, Kruus K, (2009) Essential role of the C-terminus in Melanocarpus albomyces laccase for enzyme production, catalytic properties and structure. FEBS J 276, 6285-6300.
    • (2009) FEBS J , vol.276 , pp. 6285-6300
    • Andberg, M.1    Hakulinen, N.2    Auer, S.3    Saloheimo, M.4    Koivula, A.5    Rouvinen, J.6    Kruus, K.7
  • 43
    • 77956488302 scopus 로고    scopus 로고
    • Mechanisms underlying dioxygen reduction in laccases. Structural and modelling studies focusing on proton transfer
    • doi.
    • Bento I, Silva CS, Chen Z, Martins LO, Lindley PF, &, Soares CM, (2010) Mechanisms underlying dioxygen reduction in laccases. Structural and modelling studies focusing on proton transfer. BMC Struct Biol 10, 28, doi:.
    • (2010) BMC Struct Biol , vol.10 , pp. 28
    • Bento, I.1    Silva, C.S.2    Chen, Z.3    Martins, L.O.4    Lindley, P.F.5    Soares, C.M.6
  • 45
    • 76849084273 scopus 로고    scopus 로고
    • Bio-electrochemical characterisation of high and low redox potential laccases from fungal and plant origin
    • Frasconi M, Favero G, Boer H, Koivula A, &, Mazzei F, (2010) Bio-electrochemical characterisation of high and low redox potential laccases from fungal and plant origin. Biochim Biophys Acta Proteins Proteom 1804, 899-908.
    • (2010) Biochim Biophys Acta Proteins Proteom , vol.1804 , pp. 899-908
    • Frasconi, M.1    Favero, G.2    Boer, H.3    Koivula, A.4    Mazzei, F.5
  • 46
    • 69749107876 scopus 로고    scopus 로고
    • Structure-function studies of a Melanocarpus albomyces laccase suggest a pathway for oxidation of phenolic compounds
    • Kallio JP, Auer S, Jänis J, Andberg M, Kruus K, Rouvinen J, Koivula A, &, Hakulinen N, (2009) Structure-function studies of a Melanocarpus albomyces laccase suggest a pathway for oxidation of phenolic compounds. J Mol Biol 392, 895-909.
    • (2009) J Mol Biol , vol.392 , pp. 895-909
    • Kallio, J.P.1    Auer, S.2    Jänis, J.3    Andberg, M.4    Kruus, K.5    Rouvinen, J.6    Koivula, A.7    Hakulinen, N.8
  • 47
    • 0031033309 scopus 로고    scopus 로고
    • Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases
    • Xu F, (1997) Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases. J Biol Chem 272, 924-928. (Pubitemid 27034582)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.2 , pp. 924-928
    • Xu, F.1
  • 48
    • 0036310984 scopus 로고    scopus 로고
    • Purification and characterisation of a novel laccase from the ascomycete Melanocarpus albomyces
    • DOI 10.1007/s00253-002-1012-x
    • Kiiskinen L-L, Viikari L, &, Kruus K, (2002) Purification and characterization of a novel laccase from the ascomycete Melanocarpus albomyces. Appl Microbiol Biotechnol 59, 198-204. (Pubitemid 34756959)
    • (2002) Applied Microbiology and Biotechnology , vol.59 , Issue.2-3 , pp. 198-204
    • Kiiskinen, L.-L.1    Viikari, L.2    Kruus, K.3
  • 49
    • 77649184581 scopus 로고    scopus 로고
    • Purification and characterizaion of a novel laccase from the ascomycete Trichoderma atroviride: Application on bioremediation of phenolic compounds
    • Chakroun H, Mechichi T, Martinez MJ, Dhouib A, &, Sayadi S, (2010) Purification and characterizaion of a novel laccase from the ascomycete Trichoderma atroviride: application on bioremediation of phenolic compounds. Process Biochem 45, 507-513.
    • (2010) Process Biochem , vol.45 , pp. 507-513
    • Chakroun, H.1    Mechichi, T.2    Martinez, M.J.3    Dhouib, A.4    Sayadi, S.5
  • 50
    • 33646195686 scopus 로고    scopus 로고
    • Detection of protein assemblies in crystals
    • In (Berthold M.R. ed), pp. Springer-Verlag, Berlin.
    • Krissinel E, &, Henrick K, (2005) Detection of protein assemblies in crystals. In Lecture Notes in Computer Science (, Berthold MR, ed), pp 163-174. Springer-Verlag, Berlin.
    • (2005) Lecture Notes in Computer Science , pp. 163-174
    • Krissinel, E.1    Henrick, K.2
  • 51
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E, &, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372, 774-797. (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 52
    • 72449167058 scopus 로고    scopus 로고
    • Crystal contacts as nature's docking solutions
    • Krissinel E, (2009) Crystal contacts as nature's docking solutions. J Comput Chem 31, 133-143.
    • (2009) J Comput Chem , vol.31 , pp. 133-143
    • Krissinel, E.1
  • 53
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • DOI 10.1016/S0022-2836(02)01281-0
    • Nooren MA, &, Thornton JM, (2003) Structural characterization and functional significance of transient protein-protein interactions. J Mol Biol 325, 991-1018. (Pubitemid 36263408)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.5 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 54
    • 4844228512 scopus 로고    scopus 로고
    • Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme
    • DOI 10.1099/mic.0.27147-0
    • Kiiskinen L-L, Kruus K, Bailey M, Ylosmaki E, Siika-aho M, &, Saloheimo M, (2004) Expression of Melanocarpus albomyces laccase in Trichoderma reesei and characterization of the purified enzyme. Microbiology 150, 3065-3074. (Pubitemid 39317807)
    • (2004) Microbiology , vol.150 , Issue.9 , pp. 3065-3074
    • Kiiskinen, L.-L.1    Kruus, K.2    Bailey, M.3    Ylosmaki, E.4    Siika-aho, M.5    Saloheimo, M.6
  • 55
    • 0037009169 scopus 로고    scopus 로고
    • Investigations on the laccase-catalyzed polymerization of lignin model compounds using size-exclusion HPLC
    • DOI 10.1016/S0141-0229(02)00102-3, PII S0141022902001023
    • Rittstieg K, Suurnäkki A, Suortti T, Kruus K, Guebitz G, &, Buchert J, (2002) Investigations on the laccase-catalyzed polymerization of lignin model compounds using size-exclusion HPLC. Enzyme Microbial Technol 31, 403-410. (Pubitemid 34874820)
    • (2002) Enzyme and Microbial Technology , vol.31 , Issue.4 , pp. 403-410
    • Rittstieg, K.1    Suurnakki, A.2    Suortti, T.3    Kruus, K.4    Guebitz, G.5    Buchert, J.6
  • 57
    • 0035066836 scopus 로고    scopus 로고
    • Global indicators of X-ray data quality
    • DOI 10.1107/S0021889800018227
    • Weiss M, (2001) Global indicators of X-ray data quality. J Appl Crystallogr 34, 130-135. (Pubitemid 32290301)
    • (2001) Journal of Applied Crystallography , vol.34 , Issue.2 , pp. 130-135
    • Weiss, M.S.1
  • 58
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4.
    • Collaborative Computational Project, Number 4 (1994) The CCP4 Suite: programs for protein crystallography. Acta Crystallogr D50, 760-763.
    • (1994) Acta Crystallogr , vol.50 D , pp. 760-763
  • 59
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French GS, &, Wilson KS, (1978) On the treatment of negative intensity observations. Acta Crystallogr A34, 517-525.
    • (1978) Acta Crystallogr , vol.34 A , pp. 517-525
    • French, G.S.1    Wilson, K.S.2
  • 63
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine AA, Richelle J, &, Wodak SJ, (1999) SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr D55, 191-205. (Pubitemid 29053816)
    • (1999) Acta Crystallographica Section D: Biological Crystallography , vol.55 , Issue.1 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3


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