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Volumn 60, Issue 4, 2005, Pages 598-605

Hypocrea jecorina (Trichoderma reesei) Cel7A as a molecular machine: A docking study

Author keywords

AutoDock; Brownian ratchet; Cel7a; Cellobiohydrolase; Cellulose binding domain; Docking; Hypocrea jecorina; Molecular machine; Trichoderma reesei

Indexed keywords

CELLULOSE; FUNGAL ENZYME; OLIGOSACCHARIDE; PROTEIN CEL7A; UNCLASSIFIED DRUG;

EID: 24644500001     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20547     Document Type: Article
Times cited : (54)

References (43)
  • 1
    • 24644478868 scopus 로고    scopus 로고
    • Carbohydrate-Active Enzymes server
    • Coutinho PM, Henrissat B. Carbohydrate-Active Enzymes server; 1999. http://afmb.cnrs-mrs.fr/CAZY/.
    • (1999)
    • Coutinho, P.M.1    Henrissat, B.2
  • 3
    • 0345676498 scopus 로고    scopus 로고
    • High-resolution crystal structures reveal how a cellulose chain is bound in the 50 Å long tunnel of cellobiohydrolase I from Trichoderma reesei
    • Divne C, Ståhlberg J, Teeri TT, Jones TA. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 Å long tunnel of cellobiohydrolase I from Trichoderma reesei. J Mol Biol 1998;275:309-325.
    • (1998) J Mol Biol , vol.275 , pp. 309-325
    • Divne, C.1    Ståhlberg, J.2    Teeri, T.T.3    Jones, T.A.4
  • 4
    • 0024962351 scopus 로고
    • Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei: A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
    • Kraulis J, Clore GM, Nilges M, Jones TA, Pettersson G, Knowles J, Gronenborn AM. Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry 1989;28:7241-7257.
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 6
    • 0030606294 scopus 로고    scopus 로고
    • Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei
    • Ståhlberg J, Divne C, Koivula A, Piens K, Claeyssens M, Teeri TT, Jones TA. Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei. J Mol Biol 1996;264:337-349.
    • (1996) J Mol Biol , vol.264 , pp. 337-349
    • Ståhlberg, J.1    Divne, C.2    Koivula, A.3    Piens, K.4    Claeyssens, M.5    Teeri, T.T.6    Jones, T.A.7
  • 7
    • 0343247806 scopus 로고    scopus 로고
    • The roles and function of cellulose-binding domains
    • Linder M, Teeri TT. The roles and function of cellulose-binding domains. J Biotechnol 1997;57:15-28.
    • (1997) J Biotechnol , vol.57 , pp. 15-28
    • Linder, M.1    Teeri, T.T.2
  • 8
    • 0033563990 scopus 로고    scopus 로고
    • Widely different off rates of two closely related cellulose-binding domains from Trichoderma reesei
    • Carrard G, Linder M. Widely different off rates of two closely related cellulose-binding domains from Trichoderma reesei. Eur J Biochem 1999;262:637-643.
    • (1999) Eur J Biochem , vol.262 , pp. 637-643
    • Carrard, G.1    Linder, M.2
  • 9
    • 0034641715 scopus 로고    scopus 로고
    • Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose
    • Carrard G, Koivula A, Söderlund H, Béguin P. Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose. Proc Natl Acad Sci USA 2000;97:10342-10347.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10342-10347
    • Carrard, G.1    Koivula, A.2    Söderlund, H.3    Béguin, P.4
  • 10
    • 14744278342 scopus 로고
    • A new model for enzymatic hydrolysis of cellulose based on the two-domain structure of cellobiohydrolase I
    • Ståhlberg J, Johansson G, Pettersson G. A new model for enzymatic hydrolysis of cellulose based on the two-domain structure of cellobiohydrolase I. Bio/Technology 1991;9:286-290.
    • (1991) Bio/Technology , vol.9 , pp. 286-290
    • Ståhlberg, J.1    Johansson, G.2    Pettersson, G.3
  • 12
    • 0032487130 scopus 로고    scopus 로고
    • Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei: Adsorption, sugar production pattern, and synergism of the enzymes
    • Medve J, Karlsson J, Lee D, Tjerneld F. Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei: adsorption, sugar production pattern, and synergism of the enzymes. Biotechnol Bioeng 1998;59:621-634.
    • (1998) Biotechnol Bioeng , vol.59 , pp. 621-634
    • Medve, J.1    Karlsson, J.2    Lee, D.3    Tjerneld, F.4
  • 13
    • 0031776810 scopus 로고    scopus 로고
    • The cellobiohydrolases of Trichoderma reesei: A review of indirect and direct evidence that their function is not just glycosidic bond hydrolysis
    • Sinnott ML. The cellobiohydrolases of Trichoderma reesei: a review of indirect and direct evidence that their function is not just glycosidic bond hydrolysis. Biochem Soc Trans 1998;26:160-164.
    • (1998) Biochem Soc Trans , vol.26 , pp. 160-164
    • Sinnott, M.L.1
  • 15
    • 0031058806 scopus 로고    scopus 로고
    • Automated docking of monosaccharide substrates and analogues and methyl α-acarviosinide in the glucoamylase active site
    • Coutinho PM, Dowd MK, Reilly PJ. Automated docking of monosaccharide substrates and analogues and methyl α-acarviosinide in the glucoamylase active site. Proteins 1997;27:235-248.
    • (1997) Proteins , vol.27 , pp. 235-248
    • Coutinho, P.M.1    Dowd, M.K.2    Reilly, P.J.3
  • 16
    • 0032716849 scopus 로고    scopus 로고
    • Automated docking of maltose, 2-deoxymaltose and maltotetraose into the soybean β-amylase active site
    • Laederach A, Dowd MK, Coutinho PM, Reilly PJ. Automated docking of maltose, 2-deoxymaltose and maltotetraose into the soybean β-amylase active site. Proteins 1999;37:166-175.
    • (1999) Proteins , vol.37 , pp. 166-175
    • Laederach, A.1    Dowd, M.K.2    Coutinho, P.M.3    Reilly, P.J.4
  • 17
    • 0036783337 scopus 로고    scopus 로고
    • Understanding protein structure-function relationships in Family 47 α-1,2-mannosidases through computational docking of ligands
    • Mulakala C, Reilly PJ. Understanding protein structure-function relationships in Family 47 α-1,2-mannosidases through computational docking of ligands. Proteins 2002;49:125-134.
    • (2002) Proteins , vol.49 , pp. 125-134
    • Mulakala, C.1    Reilly, P.J.2
  • 18
    • 4444357238 scopus 로고    scopus 로고
    • Arg343 in human surfactant protein D governs discrimination between glucose and N-acetylglucosamine ligands
    • Allen MJ, Laederach A, Reilly PJ, Mason RJ, Voelker DR. Arg343 in human surfactant protein D governs discrimination between glucose and N-acetylglucosamine ligands. Glycobiology 2004;14:693-700.
    • (2004) Glycobiology , vol.14 , pp. 693-700
    • Allen, M.J.1    Laederach, A.2    Reilly, P.J.3    Mason, R.J.4    Voelker, D.R.5
  • 19
    • 4444258637 scopus 로고    scopus 로고
    • Automated docking of phospholipids to the phospholipase D active site: Insight into the catalytic mechanism
    • Aikens CL, Laederach A, Reilly PJ. Automated docking of phospholipids to the phospholipase D active site: insight into the catalytic mechanism. Proteins 2004;57:27-35.
    • (2004) Proteins , vol.57 , pp. 27-35
    • Aikens, C.L.1    Laederach, A.2    Reilly, P.J.3
  • 20
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: Three related resources
    • Rodriguez R, Chinea G, Lopez N, Pons T, Vriend G. Homology modeling, model and software evaluation: three related resources. Bioinformatics 1998;14:523-528.
    • (1998) Bioinformatics , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 22
    • 24644455754 scopus 로고
    • Department of Chemistry, University of Arizona, Tucson, AZ
    • Walters P, Stahl M. Department of Chemistry, University of Arizona, Tucson, AZ. http://smog.com/chem/babel/; 1992-1996.
    • (1992)
    • Walters, P.1    Stahl, M.2
  • 23
    • 0025390935 scopus 로고
    • MOPAC: A semiempirical molecular-orbital program
    • Available online
    • Stewart JJP. MOPAC: a semiempirical molecular-orbital program. J Comput-Aided Mol Des 1990;4:1-105. Available online at http://www.webmo.net/ support/linux_binaries.html.
    • (1990) J Comput-Aided Mol des , vol.4 , pp. 1-105
    • Stewart, J.J.P.1
  • 24
    • 36048972648 scopus 로고
    • Native cellulose - A composite of two distinct crystalline forms
    • Atalla RH, Vanderhart DL. Native cellulose - a composite of two distinct crystalline forms. Science 1984;223:283-285.
    • (1984) Science , vol.223 , pp. 283-285
    • Atalla, R.H.1    Vanderhart, D.L.2
  • 25
    • 0036017874 scopus 로고    scopus 로고
    • Conformational features of crystal-surface cellulose from higher plants
    • Viëtor RJ, Newman RH, Ha MA, Apperley DC, Jarvis MC. Conformational features of crystal-surface cellulose from higher plants. Plant J 2002;30:721-731.
    • (2002) Plant J , vol.30 , pp. 721-731
    • Viëtor, R.J.1    Newman, R.H.2    Ha, M.A.3    Apperley, D.C.4    Jarvis, M.C.5
  • 26
    • 1642570259 scopus 로고    scopus 로고
    • Molecular conformations at the cellulose-water interface
    • Newman RH, Davidson TC. Molecular conformations at the cellulose-water interface. Cellulose 2004;11:23-32.
    • (2004) Cellulose , vol.11 , pp. 23-32
    • Newman, R.H.1    Davidson, T.C.2
  • 27
    • 0029856409 scopus 로고    scopus 로고
    • Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: Substrate distortion gives rise to the preferred axial orientation for the leaving group
    • Sulzenbacher G, Driguez H, Henrissat B, Schülein M, Davies GJ. Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group. Biochemistry 1996;35:15280-15287.
    • (1996) Biochemistry , vol.35 , pp. 15280-15287
    • Sulzenbacher, G.1    Driguez, H.2    Henrissat, B.3    Schülein, M.4    Davies, G.J.5
  • 28
    • 0028533340 scopus 로고
    • Modeling of aldopyranosyl ring puckering with MM3(92)
    • Dowd MK, French AD, Reilly PJ. Modeling of aldopyranosyl ring puckering with MM3(92). Carbohyd Res 1994;264:1-19.
    • (1994) Carbohyd Res , vol.264 , pp. 1-19
    • Dowd, M.K.1    French, A.D.2    Reilly, P.J.3
  • 30
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas N. Atomic features of protein-carbohydrate interactions. Curr Opin Struct Biol 1991;1:732-740.
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 732-740
    • Vyas, N.1
  • 33
    • 0033979485 scopus 로고    scopus 로고
    • The mechanism of cellulase action on cotton fibers: Evidence from atomic force microscopy
    • Lee I, Evans BR, Woodward J. The mechanism of cellulase action on cotton fibers: evidence from atomic force microscopy. Ultramicroscopy 2000;82:213-221.
    • (2000) Ultramicroscopy , vol.82 , pp. 213-221
    • Lee, I.1    Evans, B.R.2    Woodward, J.3
  • 34
    • 0030825785 scopus 로고    scopus 로고
    • Surface diffusion of cellulases and their isolated binding domains on cellulose
    • Jervis EJ, Haynes CA, Kilburn DG. Surface diffusion of cellulases and their isolated binding domains on cellulose. J Biol Chem 1997;272:24016-24023.
    • (1997) J Biol Chem , vol.272 , pp. 24016-24023
    • Jervis, E.J.1    Haynes, C.A.2    Kilburn, D.G.3
  • 35
    • 0042099120 scopus 로고    scopus 로고
    • Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and linker sequence of cellobiohydrolase I from Penicillium janthinellum
    • Gao PJ, Chen GJ, Wang TH, Zhang YS, Liu J. Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and linker sequence of cellobiohydrolase I from Penicillium janthinellum. Acta Biochim Biophys Sinica 2001;33:13-18.
    • (2001) Acta Biochim Biophys Sinica , vol.33 , pp. 13-18
    • Gao, P.J.1    Chen, G.J.2    Wang, T.H.3    Zhang, Y.S.4    Liu, J.5
  • 36
    • 1442309235 scopus 로고    scopus 로고
    • Brownian motion, molecular motors and ratchets
    • Gabrys BJ, Pesz K, Bartkiewicz SJ. Brownian motion, molecular motors and ratchets. Physica A 2004;336:112-122.
    • (2004) Physica A , vol.336 , pp. 112-122
    • Gabrys, B.J.1    Pesz, K.2    Bartkiewicz, S.J.3
  • 37
    • 0027372765 scopus 로고
    • Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase I in its interaction with crystalline cellulose
    • Srisodsuk M, Reinikainen T, Penttila M, Teeri TT. Role of the interdomain linker peptide of Trichoderma reesei cellobiohydrolase I in its interaction with crystalline cellulose. J Biol Chem 1993;268:20756-20761.
    • (1993) J Biol Chem , vol.268 , pp. 20756-20761
    • Srisodsuk, M.1    Reinikainen, T.2    Penttila, M.3    Teeri, T.T.4
  • 38
    • 0001188346 scopus 로고
    • Structural and functional domains of cellobiohydrolase I from Trichoderma reesei: A small-angle X-ray scattering study of the intact enzyme and its core
    • Abuja PM, Schmuck M, Pilz I, Tomme P, Claeyssens M, Esterbauer H. Structural and functional domains of cellobiohydrolase I from Trichoderma reesei: a small-angle X-ray scattering study of the intact enzyme and its core. Eur Biophys J Biophys Lett 1988;15:339-342.
    • (1988) Eur Biophys J Biophys Lett , vol.15 , pp. 339-342
    • Abuja, P.M.1    Schmuck, M.2    Pilz, I.3    Tomme, P.4    Claeyssens, M.5    Esterbauer, H.6
  • 39
    • 0025923034 scopus 로고
    • Deletion of the linker connecting the catalytic and cellulose-binding domains of endoglucanase a (CenA) of Cellulomonas fimi alters its conformation and catalytic activity
    • Shen H, Schmuck M, Pilz I, Gilkes NR, Kilburn DG, Miller RC, Warren RAJ. Deletion of the linker connecting the catalytic and cellulose-binding domains of endoglucanase A (CenA) of Cellulomonas fimi alters its conformation and catalytic activity. J Biol Chem 1991;266:11335-11340.
    • (1991) J Biol Chem , vol.266 , pp. 11335-11340
    • Shen, H.1    Schmuck, M.2    Pilz, I.3    Gilkes, N.R.4    Kilburn, D.G.5    Miller, R.C.6    Raj, W.7
  • 40
    • 0024603248 scopus 로고
    • Thermodynamics of hydrolysis of disaccharides-cellobiose, gentiobiose, isomaltose, and maltose
    • Tewari YB, Goldberg RN. Thermodynamics of hydrolysis of disaccharides-cellobiose, gentiobiose, isomaltose, and maltose. J Biol Chem 1989;264:3966-3971.
    • (1989) J Biol Chem , vol.264 , pp. 3966-3971
    • Tewari, Y.B.1    Goldberg, R.N.2
  • 41
    • 0027716645 scopus 로고
    • Meaning of energetic parameters
    • Kammermeier H. Meaning of energetic parameters. Basic Res Cardiol 1993;88:380-384.
    • (1993) Basic Res Cardiol , vol.88 , pp. 380-384
    • Kammermeier, H.1
  • 42
    • 0028152402 scopus 로고
    • Cellulose hydrolysis by the cellulases from Trichoderma reesei: Adsorptions of two cellobiohydrolases, two endocellulases and their core proteins on filter-paper and their relation to hydrolysis
    • Nidetzky B, Steiner W, Claeyssens M. Cellulose hydrolysis by the cellulases from Trichoderma reesei: adsorptions of two cellobiohydrolases, two endocellulases and their core proteins on filter-paper and their relation to hydrolysis. Biochem J 1994;303:817-823.
    • (1994) Biochem J , vol.303 , pp. 817-823
    • Nidetzky, B.1    Steiner, W.2    Claeyssens, M.3
  • 43
    • 0036880196 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolecular machines: Part I. Structures and properties of isolated helicases
    • Delagoutte E, von Hippel PH. Helicase mechanisms and the coupling of helicases within macromolecular machines: Part I. Structures and properties of isolated helicases. Quart Rev Biophys 2002;35:431-478.
    • (2002) Quart Rev Biophys , vol.35 , pp. 431-478
    • Delagoutte, E.1    Von Hippel, P.H.2


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