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Volumn 8, Issue 12, 2013, Pages

Structure and function of a novel cellulase 5 from sugarcane soil metagenome

Author keywords

[No Author keywords available]

Indexed keywords

BETA GLUCAN; CARBOXYMETHYLCELLULOSE; CELE1 PROTEIN; CELLULASE; GLYCOSIDASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 84892916358     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0083635     Document Type: Article
Times cited : (59)

References (42)
  • 1
    • 19144366814 scopus 로고    scopus 로고
    • Metagenomics and industrial applications
    • doi:10.1038/nrmicro1161. PubMed: 15931168
    • Lorenz P, Eck J (2005) Metagenomics and industrial applications. Nat Rev Microbiol 3: 510-516. doi:10.1038/nrmicro1161. PubMed: 15931168.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 510-516
    • Lorenz, P.1    Eck, J.2
  • 2
    • 31544462628 scopus 로고    scopus 로고
    • Ethanol can contribute to energy and environmental goals
    • doi:10.1126/science.1121416. PubMed: 16439656
    • Farrell AE, Plevin RJ, Turner BT, Jones AD, O'Hare M et al. (2006) Ethanol can contribute to energy and environmental goals. Science 311: 506-508. doi:10.1126/science.1121416. PubMed: 16439656.
    • (2006) Science , vol.311 , pp. 506-508
    • Farrell, A.E.1    Plevin, R.J.2    Turner, B.T.3    Jones, A.D.4    O'Hare, M.5
  • 3
    • 67649819695 scopus 로고    scopus 로고
    • New improvements for lignocellulosic ethanol
    • doi:10.1016/j.copbio.2009.05.009. PubMed: 19502048
    • Margeot A, Hahn-Hagerdal B, Edlund M, Slade R, Monot F (2009) New improvements for lignocellulosic ethanol. Curr Opin Biotechnol 20: 372-380. doi:10.1016/j.copbio.2009.05.009. PubMed: 19502048.
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 372-380
    • Margeot, A.1    Hahn-Hagerdal, B.2    Edlund, M.3    Slade, R.4    Monot, F.5
  • 4
    • 70349765870 scopus 로고    scopus 로고
    • Protein engineering in designing tailored enzymes and microorganisms for biofuels production
    • doi:10.1016/j.copbio.2009.07.001. PubMed: 19660930
    • Wen F, Nair NU, Zhao H (2009) Protein engineering in designing tailored enzymes and microorganisms for biofuels production. Curr Opin Biotechnol 20: 412-419. doi:10.1016/j.copbio.2009.07.001. PubMed: 19660930.
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 412-419
    • Wen, F.1    Nair, N.U.2    Zhao, H.3
  • 5
    • 43749091376 scopus 로고    scopus 로고
    • Structure, organization, and functions of cellulose synthase complexes in higher plants
    • Festucci-Buselli RA, Otoni WC, Joshi CP (2007) Structure, organization, and functions of cellulose synthase complexes in higher plants. Braz J Plant Physiol 19: 1-13.
    • (2007) Braz J Plant Physiol , vol.19 , pp. 1-13
    • Festucci-Buselli, R.A.1    Otoni, W.C.2    Joshi, C.P.3
  • 6
    • 68349130056 scopus 로고    scopus 로고
    • Structure of endoglucanase Cel9A from the thermoacidophilic Alicyclobacillus acidocaldarius
    • doi:10.1107/S0907444909012773. PubMed: 19622857
    • Pereira JH, Sapra R, Volponi JV, Kozina CL, Simmons B et al. (2009) Structure of endoglucanase Cel9A from the thermoacidophilic Alicyclobacillus acidocaldarius. Acta Crystallogr D Biol Crystallogr 65: 744-750. doi:10.1107/S0907444909012773. PubMed: 19622857.
    • (2009) Acta Crystallogr D Biol Crystallogr , vol.65 , pp. 744-750
    • Pereira, J.H.1    Sapra, R.2    Volponi, J.V.3    Kozina, C.L.4    Simmons, B.5
  • 7
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • PubMed: 8352747
    • Henrissat B, Bairoch A (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 293 (3): 781-788. PubMed: 8352747.
    • (1993) Biochem J , vol.293 , Issue.3 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 8
    • 84880808378 scopus 로고    scopus 로고
    • Development and Biotechnological Application of a Novel Endoxylanase Family GH10 Identified from Sugarcane Soil Metagenome
    • PubMed: 23922891
    • Alvarez TM, Goldbeck R, Dos Santos CR, Paixão DA, Gonçalves TA et al. (2013) Development and Biotechnological Application of a Novel Endoxylanase Family GH10 Identified from Sugarcane Soil Metagenome. PLOS ONE, 8: e70014. PubMed: 23922891.
    • (2013) PLOS ONE , vol.8
    • Alvarez, T.M.1    Goldbeck, R.2    Dos Santos, C.R.3    Paixão, D.A.4    Gonçalves, T.A.5
  • 9
    • 0020032328 scopus 로고
    • Use of Congo red-polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from the bovine rumen
    • PubMed: 7081984
    • Teather RM, Wood PJ (1982) Use of Congo red-polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from the bovine rumen. Appl Environ Microbiol 43: 777-780. PubMed: 7081984.
    • (1982) Appl Environ Microbiol , vol.43 , pp. 777-780
    • Teather, R.M.1    Wood, P.J.2
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • doi: 10.1038/227680a0. PubMed: 5432063
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685. doi: 10.1038/227680a0. PubMed: 5432063.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • doi:10.1021/ac60147a030
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31: 426-428. doi:10.1021/ac60147a030.
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 12
    • 0001369336 scopus 로고
    • A buffer solution for colorimetric comparison
    • McIlvaine TC (1921) A buffer solution for colorimetric comparison. J Biol Chem 49: 183-186.
    • (1921) J Biol Chem , vol.49 , pp. 183-186
    • McIlvaine, T.C.1
  • 13
    • 79953029268 scopus 로고    scopus 로고
    • Mode of operation and low-resolution structure of a multidomain and hyperthermophilic endo-beta-1,3-glucanase from Thermotoga petrophila
    • doi:10.1016/j.bbrc.2011.02.098. PubMed: 21352806
    • Cota J, Alvarez TM, Citadini AP, Santos CR, de Oliveira Neto M et al. (2011) Mode of operation and low-resolution structure of a multidomain and hyperthermophilic endo-beta-1,3-glucanase from Thermotoga petrophila. Biochem Biophys Res Commun 406: 590-594. doi:10.1016/j.bbrc.2011.02.098. PubMed: 21352806.
    • (2011) Biochem Biophys Res Commun , vol.406 , pp. 590-594
    • Cota, J.1    Alvarez, T.M.2    Citadini, A.P.3    Santos, C.R.4    De Oliveira Neto, M.5
  • 14
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • doi: 10.1093/nar/gkh371. PubMed: 15215473
    • Whitmore L, Wallace BA (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32: W668-W673. doi: 10.1093/nar/gkh371. PubMed: 15215473.
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 15
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • doi:10.1002/bip.20853. PubMed: 17896349
    • Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89: 392-400. doi:10.1002/bip.20853. PubMed: 17896349.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 16
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • doi:10.1016/0022-2836(68)90205-2. PubMed: 5700707
    • Matthews BW (1968) Solvent content of protein crystals. J Mol Biol 33: 491-497. doi:10.1016/0022-2836(68)90205-2. PubMed: 5700707.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 17
    • 74549194551 scopus 로고    scopus 로고
    • Molecular replacement with MOLREP
    • doi:10.1107/S0907444909042589. PubMed: 20057045
    • Vagin A, Teplyakov A (2010) Molecular replacement with MOLREP. Acta Crystallogr D Biol Crystallogr 66: 22-25. doi:10.1107/S0907444909042589. PubMed: 20057045.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 22-25
    • Vagin, A.1    Teplyakov, A.2
  • 18
    • 18044372844 scopus 로고    scopus 로고
    • Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering
    • doi:10.1016/j.jmb.2005.03.026. PubMed: 15854656
    • Violot S, Aghajari N, Czjzek M, Feller G, Sonan GK et al. (2005) Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering. J Mol Biol 348: 1211-1224. doi:10.1016/j.jmb.2005.03.026. PubMed: 15854656.
    • (2005) J Mol Biol , vol.348 , pp. 1211-1224
    • Violot, S.1    Aghajari, N.2    Czjzek, M.3    Feller, G.4    Sonan, G.K.5
  • 19
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • doi:10.1107/S0907444911001314. PubMed: 21460454
    • Murshudov GN, Skubák P, Lebedev AA, Pannu NS, Steiner RA et al. (2011) REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67: 355-367. doi:10.1107/S0907444911001314. PubMed: 21460454.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 355-367
    • Murshudov, G.N.1    Skubák, P.2    Lebedev, A.A.3    Pannu, N.S.4    Steiner, R.A.5
  • 20
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • doi: 10.1107/S0907444904019158. PubMed: 15572765
    • Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132. doi: 10.1107/S0907444904019158. PubMed: 15572765.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 21
    • 79955038539 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of cellulose by the cellobiohydrolase domain of CelB from the hyperthermophilic bacterium Caldicellulosiruptor saccharolyticus
    • doi:10.1016/j.biortech.2011.02.036. PubMed: 21421309
    • Park JI, Kent MS, Datta S, Holmes BM, Huang Z et al. (2011) Enzymatic hydrolysis of cellulose by the cellobiohydrolase domain of CelB from the hyperthermophilic bacterium Caldicellulosiruptor saccharolyticus. Bioresour Technol 102: 5988-5994. doi:10.1016/j.biortech.2011.02.036. PubMed: 21421309.
    • (2011) Bioresour Technol , vol.102 , pp. 5988-5994
    • Park, J.I.1    Kent, M.S.2    Datta, S.3    Holmes, B.M.4    Huang, Z.5
  • 22
    • 79952535116 scopus 로고    scopus 로고
    • Cloning and functional characterization of a novel endo-beta-1,4- glucanase gene from a soil-derived metagenomic library
    • doi:10.1007/s00253-010-2828-4. PubMed: 20938774
    • Liu J, Liu WD, Zhao XL, Shen WJ, Cao H et al. (2011) Cloning and functional characterization of a novel endo-beta-1,4-glucanase gene from a soil-derived metagenomic library. Appl Microbiol Biotechnol 89: 1083-1092. doi:10.1007/s00253-010-2828-4. PubMed: 20938774.
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 1083-1092
    • Liu, J.1    Liu, W.D.2    Zhao, X.L.3    Shen, W.J.4    Cao, H.5
  • 23
    • 84055185201 scopus 로고    scopus 로고
    • Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168
    • doi:10.1042/BJ20110869. PubMed: 21880019
    • Santos CR, Paiva JH, Sforça ML, Neves JL, Navarro RZ et al. (2012) Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168. Biochem J 441: 95-104. doi:10.1042/BJ20110869. PubMed: 21880019.
    • (2012) Biochem J , vol.441 , pp. 95-104
    • Santos, C.R.1    Paiva, J.H.2    Sforça, M.L.3    Neves, J.L.4    Navarro, R.Z.5
  • 24
    • 84862743750 scopus 로고    scopus 로고
    • Identification and characterization of a cellulase-encoding gene from the buffalo rumen metagenomic library
    • PubMed: 22790926
    • Nguyen NH, Maruset L, Uengwetwanit T, Mhuantong W, Harnpicharnchai P et al. (2012) Identification and characterization of a cellulase-encoding gene from the buffalo rumen metagenomic library. Biosci Biotechnol Biochem 76: 1075-1084. PubMed: 22790926.
    • (2012) Biosci Biotechnol Biochem , vol.76 , pp. 1075-1084
    • Nguyen, N.H.1    Maruset, L.2    Uengwetwanit, T.3    Mhuantong, W.4    Harnpicharnchai, P.5
  • 25
    • 0029645407 scopus 로고
    • Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5
    • doi:10.1016/S0969-2126(01)00228-3. PubMed: 8535787
    • Ducros V, Czjzek M, Belaich A, Gaudin C, Fierobe HP et al. (1995) Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5. Structure 3: 939-949. doi:10.1016/S0969-2126(01)00228-3. PubMed: 8535787.
    • (1995) Structure , vol.3 , pp. 939-949
    • Ducros, V.1    Czjzek, M.2    Belaich, A.3    Gaudin, C.4    Fierobe, H.P.5
  • 26
    • 33748997640 scopus 로고    scopus 로고
    • Purification and characterization of a family 5 endoglucanase from a moderately thermophilic strain of Bacillus licheniformis
    • doi:10.1007/s10529-006-9153-0. PubMed: 16900329
    • Bischoff KM, Rooney AP, Li XL, Liu S, Hughes SR (2006) Purification and characterization of a family 5 endoglucanase from a moderately thermophilic strain of Bacillus licheniformis. Biotechnol Lett 28: 1761-1765. doi:10.1007/s10529-006-9153-0. PubMed: 16900329.
    • (2006) Biotechnol Lett , vol.28 , pp. 1761-1765
    • Bischoff, K.M.1    Rooney, A.P.2    Li, X.L.3    Liu, S.4    Hughes, S.R.5
  • 27
    • 78651083397 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable and halo-tolerant endoglucanase from Thermoanaerobacter tengcongensis MB4
    • doi:10.1007/s00253-010-2842-6. PubMed: 20803139
    • Liang C, Xue Y, Fioroni M, Rodríguez-Ropero F, Zhou C et al. (2011) Cloning and characterization of a thermostable and halo-tolerant endoglucanase from Thermoanaerobacter tengcongensis MB4. Appl Microbiol Biotechnol 89: 315-326. doi:10.1007/s00253-010-2842-6. PubMed: 20803139.
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 315-326
    • Liang, C.1    Xue, Y.2    Fioroni, M.3    Rodríguez-Ropero, F.4    Zhou, C.5
  • 28
    • 84860451743 scopus 로고    scopus 로고
    • A salt-bridge controlled by ligand binding modulates the hydrolysis reaction in a GH5 endoglucanase
    • doi:10.1093/protein/gzs010. PubMed: 22419828
    • Badieyan S, Bevan DR, Zhang C (2012) A salt-bridge controlled by ligand binding modulates the hydrolysis reaction in a GH5 endoglucanase. Protein Eng Des Sel 25: 223-233. doi:10.1093/protein/gzs010. PubMed: 22419828.
    • (2012) Protein Eng des Sel , vol.25 , pp. 223-233
    • Badieyan, S.1    Bevan, D.R.2    Zhang, C.3
  • 29
    • 0026562198 scopus 로고
    • Stereochemistry of the hydrolysis reaction catalyzed by endoglucanase Z from Erwinia chrysanthemi
    • doi: 10.1016/0014-5793(92)80183-H. PubMed: 1563515
    • Barras F, Bortoli-German I, Bauzan M, Rouvier J, Gey C et al. (1992) Stereochemistry of the hydrolysis reaction catalyzed by endoglucanase Z from Erwinia chrysanthemi. FEBS Lett 300: 145-148. doi: 10.1016/0014-5793(92)80183-H. PubMed: 1563515.
    • (1992) FEBS Lett , vol.300 , pp. 145-148
    • Barras, F.1    Bortoli-German, I.2    Bauzan, M.3    Rouvier, J.4    Gey, C.5
  • 30
    • 18444373877 scopus 로고    scopus 로고
    • Processive endoglucanase active in crystalline cellulose hydrolysis by the brown rot basidiomycete Gloeophyllum trabeum
    • doi: 10.1128/AEM.71.5.2412-2417.2005. PubMed: 15870328
    • Cohen R, Suzuki MR, Hammel KE (2005) Processive endoglucanase active in crystalline cellulose hydrolysis by the brown rot basidiomycete Gloeophyllum trabeum. Appl Environ Microbiol 71: 2412-2417. doi: 10.1128/AEM.71.5.2412-2417. 2005. PubMed: 15870328.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 2412-2417
    • Cohen, R.1    Suzuki, M.R.2    Hammel, K.E.3
  • 31
    • 84883277762 scopus 로고    scopus 로고
    • Deciphering the synergism of endogenous glycoside hydrolase families 1 and 9 from Coptotermes gestroi
    • doi:10.1016/j.ibmb.2013.07.007. PubMed: 23917163
    • Franco Cairo JP, Oliveira LC, Uchima CA, Alvarez TM, Citadini AP et al. (2013) Deciphering the synergism of endogenous glycoside hydrolase families 1 and 9 from Coptotermes gestroi. Insect Biochem Mol Biol 43: 970-981. doi:10.1016/j.ibmb.2013.07.007. PubMed: 23917163.
    • (2013) Insect Biochem Mol Biol , vol.43 , pp. 970-981
    • Franco Cairo, J.P.1    Oliveira, L.C.2    Uchima, C.A.3    Alvarez, T.M.4    Citadini, A.P.5
  • 32
    • 35048812937 scopus 로고    scopus 로고
    • The linker region plays a key role in the adaptation to cold of the cellulase from an Antarctic bacterium
    • doi:10.1042/BJ20070640. PubMed: 17635108
    • Sonan GK, Receveur-Brechot V, Duez C, Aghajari N, Czjzek M, Haser R, Gerday C (2007) The linker region plays a key role in the adaptation to cold of the cellulase from an Antarctic bacterium. Biochem J 407: 293-302. doi:10.1042/BJ20070640. PubMed: 17635108.
    • (2007) Biochem J , vol.407 , pp. 293-302
    • Sonan, G.K.1    Receveur-Brechot, V.2    Duez, C.3    Aghajari, N.4    Czjzek, M.5    Haser, R.6    Gerday, C.7
  • 33
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • doi:10.1016/j.jmb.2007.05.022. PubMed: 17681537
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797. doi:10.1016/j.jmb.2007.05.022. PubMed: 17681537.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 34
    • 0001590330 scopus 로고
    • The TIM barrel-the most frequently occurring folding motif in proteins
    • doi: 10.1016/0959-440X(91)90094-A
    • Brändén C-I (1991) The TIM barrel-the most frequently occurring folding motif in proteins. Curr Opin Struct Biol 1: 978-983. doi: 10.1016/0959-440X(91)90094-A.
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 978-983
    • Brändén, C.-I.1
  • 35
    • 0035958760 scopus 로고    scopus 로고
    • Type II protein secretion in gram-negative pathogenic bacteria: The study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi
    • doi:10.1006/jmbi.2001.4787. PubMed: 11501995
    • Chapon V, Czjzek M, El Hassouni M, Py B, Juy M et al. (2001) Type II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi. J Mol Biol 310: 1055-1066. doi:10.1006/jmbi.2001.4787. PubMed: 11501995.
    • (2001) J Mol Biol , vol.310 , pp. 1055-1066
    • Chapon, V.1    Czjzek, M.2    El Hassouni, M.3    Py, B.4    Juy, M.5
  • 36
    • 0036299040 scopus 로고    scopus 로고
    • A novel combination of two classic catalytic schemes
    • doi:10.1016/S0022-2836(02)00387-X. PubMed: 12079387
    • Shaw A, Bott R, Vonrhein C, Bricogne G, Power S et al. (2002) A novel combination of two classic catalytic schemes. J Mol Biol 320: 303-309. doi:10.1016/S0022-2836(02)00387-X. PubMed: 12079387.
    • (2002) J Mol Biol , vol.320 , pp. 303-309
    • Shaw, A.1    Bott, R.2    Vonrhein, C.3    Bricogne, G.4    Power, S.5
  • 37
    • 0032539533 scopus 로고    scopus 로고
    • Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A and its cellobiose complex at 2.0 A resolution
    • doi:10.1021/bi972162m. PubMed: 9485319
    • Davies GJ, Dauter M, Brzozowski AM, Bjørnvad ME, Andersen KV et al. (1998) Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A and its cellobiose complex at 2.0 A resolution. Biochemistry 37: 1926-1932. doi:10.1021/bi972162m. PubMed: 9485319.
    • (1998) Biochemistry , vol.37 , pp. 1926-1932
    • Davies, G.J.1    Dauter, M.2    Brzozowski, A.M.3    Bjørnvad, M.E.4    Andersen, K.V.5
  • 38
    • 0035958721 scopus 로고    scopus 로고
    • Crystal structure of alkaline cellulase K: Insight into the alkaline adaptation of an industrial enzyme
    • doi:10.1006/jmbi.2001.4835. PubMed: 11501997
    • Shirai T, Ishida H, Noda J, Yamane T, Ozaki K et al. (2001) Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme. J Mol Biol 310: 1079-1087. doi:10.1006/jmbi.2001.4835. PubMed: 11501997.
    • (2001) J Mol Biol , vol.310 , pp. 1079-1087
    • Shirai, T.1    Ishida, H.2    Noda, J.3    Yamane, T.4    Ozaki, K.5
  • 39
    • 0029156053 scopus 로고
    • A common protein fold and similar active site in two distinct families of beta-glycanases
    • doi:10.1038/nsb0795-569. PubMed: 7664125
    • Dominguez R, Souchon H, Spinelli S, Dauter Z, Wilson KS et al. (1995) A common protein fold and similar active site in two distinct families of beta-glycanases. Nat Struct Biol 2: 569-576. doi:10.1038/nsb0795-569. PubMed: 7664125.
    • (1995) Nat Struct Biol , vol.2 , pp. 569-576
    • Dominguez, R.1    Souchon, H.2    Spinelli, S.3    Dauter, Z.4    Wilson, K.S.5
  • 40
    • 0029740205 scopus 로고    scopus 로고
    • Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose
    • doi:10.1021/bi9604439. PubMed: 8718854
    • Sakon J, Adney WS, Himmel ME, Thomas SR, Karplus PA (1996) Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose. Biochemistry 35: 10648-10660. doi:10.1021/bi9604439. PubMed: 8718854.
    • (1996) Biochemistry , vol.35 , pp. 10648-10660
    • Sakon, J.1    Adney, W.S.2    Himmel, M.E.3    Thomas, S.R.4    Karplus, P.A.5
  • 41
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas NK (1991) Atomic features of protein-carbohydrate interactions. Curr Opin Struct Biol 1: 723-740.
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 723-740
    • Vyas, N.K.1
  • 42
    • 0034737321 scopus 로고    scopus 로고
    • Insights into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form
    • doi: 10.1006/jmbi.2000.3567. PubMed: 10731432
    • Varrot A, Schülein M, Davies GJ (2000) Insights into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form. J Mol Biol 297: 819-828. doi: 10.1006/jmbi.2000.3567. PubMed: 10731432.
    • (2000) J Mol Biol , vol.297 , pp. 819-828
    • Varrot, A.1    Schülein, M.2    Davies, G.J.3


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