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Volumn 17, Issue 19, 1998, Pages 5551-5562

The crystal structure of the processive endocellulase CelF of Clostridium cellulolyticum in complex with a thiooligosaccharide inhibitor at 2.0 Å resolution

Author keywords

Cellulase; Crystal structure; Family 48 glycosyl hydrolase; Processive endo action; Thiooligosaccharide inhibitor

Indexed keywords

ASPARTIC ACID; CELLULASE; CELLULOSE; GLUTAMIC ACID; GLYCOSIDASE; MULTIENZYME COMPLEX; OLIGOSACCHARIDE;

EID: 0032190381     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.19.5551     Document Type: Article
Times cited : (114)

References (75)
  • 1
    • 0031910806 scopus 로고    scopus 로고
    • Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor
    • Aghajari, N., Feller, G., Gerday, Ch. and Haser, R. (1998) Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Sci., 7, 564-572.
    • (1998) Protein Sci. , vol.7 , pp. 564-572
    • Aghajari, N.1    Feller, G.2    Gerday, Ch.3    Haser, R.4
  • 2
    • 0026726797 scopus 로고
    • Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2 Å
    • Aleshin, A., Golubev, A., Firsov, L.M. and Honzatko, R.B. (1992) Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2 Å. J. Biol. Chem., 267, 19291-19298.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19291-19298
    • Aleshin, A.1    Golubev, A.2    Firsov, L.M.3    Honzatko, R.B.4
  • 3
    • 0030584665 scopus 로고    scopus 로고
    • The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermaceilum
    • Alzari, P.M., Souchon, H. and Dominguez, R. (1996) The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermaceilum. Structure, 4, 265-275.
    • (1996) Structure , vol.4 , pp. 265-275
    • Alzari, P.M.1    Souchon, H.2    Dominguez, R.3
  • 4
    • 0026739086 scopus 로고
    • Sequence analysis of a gene cluster encoding cellulases from Clostridium cellulolyticum
    • Bagnara-Tardif, C., Gaudin, C., Belaich, A., Hoest, P., Citard, T. and Belaich, J.P. (1992) Sequence analysis of a gene cluster encoding cellulases from Clostridium cellulolyticum. Gene, 119, 17-28.
    • (1992) Gene , vol.119 , pp. 17-28
    • Bagnara-Tardif, C.1    Gaudin, C.2    Belaich, A.3    Hoest, P.4    Citard, T.5    Belaich, J.P.6
  • 5
    • 0030065736 scopus 로고    scopus 로고
    • Identification of two functionally different classes of exocellulases
    • Barr, B.K., Hsieh, Y.L., Ganem, B. and Wilson, D.B. (1996) Identification of two functionally different classes of exocellulases. Biochemistry, 35, 586-592.
    • (1996) Biochemistry , vol.35 , pp. 586-592
    • Barr, B.K.1    Hsieh, Y.L.2    Ganem, B.3    Wilson, D.B.4
  • 6
    • 0027984011 scopus 로고
    • The cellulosome - A treasure trove for biotechnology
    • Bayer, E.A., Morag, E. and Lamed, R. (1994) The cellulosome - a treasure trove for biotechnology. Trends Biotechnol., 12, 379-386.
    • (1994) Trends Biotechnol. , vol.12 , pp. 379-386
    • Bayer, E.A.1    Morag, E.2    Lamed, R.3
  • 8
    • 0025779380 scopus 로고
    • Purification and properties of a novel type of exo-1,4-beta-glucanase (Avicelase II) from the cellulolytic thermophile Clostridium stercorarium
    • Bronnenmeier, K., Rucknagel, K.P. and Staudenbauer, W.L. (1991) Purification and properties of a novel type of exo-1,4-beta-glucanase (Avicelase II) from the cellulolytic thermophile Clostridium stercorarium. Eur. J. Biochem., 200, 379-385.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 379-385
    • Bronnenmeier, K.1    Rucknagel, K.P.2    Staudenbauer, W.L.3
  • 9
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992) The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 10
    • 84944812221 scopus 로고
    • Slow cooling protocols for crystallographic refinement by simulated annealing
    • Brünger, A.T. and Kurkowski, A. (1990) Slow cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr. Sect. A, 46, 46-57.
    • (1990) Acta Crystallogr. Sect. A , vol.46 , pp. 46-57
    • Brünger, A.T.1    Kurkowski, A.2
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. Sect. D, 50, 760-763.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 12
    • 0002831168 scopus 로고
    • Cellulose degradation by Fungi
    • Fogarty, W.M. and Kely, C.T. (eds), Elsevier Applied Science, London, UK
    • Coughlan, M. (1990) Cellulose degradation by Fungi. In Fogarty, W.M. and Kely, C.T. (eds), Microbial Enzymes and Biotechnology. Elsevier Applied Science, London, UK, pp. 1-36.
    • (1990) Microbial Enzymes and Biotechnology , pp. 1-36
    • Coughlan, M.1
  • 13
    • 0002583957 scopus 로고
    • 'Dm': An automated procedure for phase improvement by density modification
    • Cowtan, K. (1994) 'Dm': an automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newslett., 31, 34-38.
    • (1994) Joint CCP4 ESF-EACBM Newslett. , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 14
    • 0021056189 scopus 로고
    • Characterization of exoglucanase and synergistic hydrolysis of cellulose of Clostridium stercorarium
    • Creuzet, N., Berenger, J.F. and Frixon, C. (1983) Characterization of exoglucanase and synergistic hydrolysis of cellulose of Clostridium stercorarium. FEMS Microbiol. Lett., 20, 347-350.
    • (1983) FEMS Microbiol. Lett. , vol.20 , pp. 347-350
    • Creuzet, N.1    Berenger, J.F.2    Frixon, C.3
  • 15
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies, G.J. and Henrissat, B. (1995) Structures and mechanisms of glycosyl hydrolases. Structure, 3, 853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.J.1    Henrissat, B.2
  • 16
    • 0010322763 scopus 로고
    • Structural studies on fungal endoglucanases from Humicola insolens
    • Petersen, S.B., Svensson, B. and Pedersen, S. (eds), Elsevier Science B.V., Amsterdam, The Netherlands
    • Davies, G.J. and Schülein, M. (1995) Structural studies on fungal endoglucanases from Humicola insolens. In Petersen, S.B., Svensson, B. and Pedersen, S. (eds), Carbohydrate Bioengineering. Elsevier Science B.V., Amsterdam, The Netherlands, pp. 232-235.
    • (1995) Carbohydrate Bioengineering , pp. 232-235
    • Davies, G.J.1    Schülein, M.2
  • 17
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies, G.J., Wilson, K.S. and Henrissat, B. (1997) Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J., 321, 557-559.
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 19
    • 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, T.T. and Jones, T.A. (1998) 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., 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
  • 22
    • 0008148883 scopus 로고
    • Stereochemical investigation of, 2,3,4,6-Tetra-O-acetyl-1-S-benzhydroximoyl-α-D-glucopyranose
    • Durier, V. and Driguez, H. (1992) Stereochemical investigation of, 2,3,4,6-Tetra-O-acetyl-1-S-benzhydroximoyl-α-D-glucopyranose. Acta Crystallogr. Sect. C, 48, 1791-1794.
    • (1992) Acta Crystallogr. Sect. C , vol.48 , pp. 1791-1794
    • Durier, V.1    Driguez, H.2
  • 23
    • 0029644059 scopus 로고    scopus 로고
    • Crystal structure of various maltooligosaccharides bound to maltoporin reveal a specific translocation pathway
    • Dutzler, R., Wang, Y.-F., Rizkallah, P.J., Rosenbusch, J.P. and Schirmer, T. (1996) Crystal structure of various maltooligosaccharides bound to maltoporin reveal a specific translocation pathway. Structure, 4, 127-134.
    • (1996) Structure , vol.4 , pp. 127-134
    • Dutzler, R.1    Wang, Y.-F.2    Rizkallah, P.J.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 24
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein-structure refinement
    • Engh, R.A. and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein-structure refinement. Acta Crystallogr. Sect. A, 47, 392-400.
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 25
    • 0024802393 scopus 로고
    • Sequence analysis of the Clostridium cellulolyticum endoglucanase-A-encoding gene, celCCA
    • Faure, E., Belaich, A., Bagnara, C., Gaudin, C. and Belaich, J.P. (1989) Sequence analysis of the Clostridium cellulolyticum endoglucanase-A-encoding gene, celCCA. Gene, 84, 39-46.
    • (1989) Gene , vol.84 , pp. 39-46
    • Faure, E.1    Belaich, A.2    Bagnara, C.3    Gaudin, C.4    Belaich, J.P.5
  • 26
    • 0029070171 scopus 로고
    • Omega loops: Nonregular secundary structures significant in protein function and stability
    • Fetrow, J.S. (1995) Omega loops: nonregular secundary structures significant in protein function and stability. FASEB J., 9, 708-717.
    • (1995) FASEB J. , vol.9 , pp. 708-717
    • Fetrow, J.S.1
  • 28
    • 0027493384 scopus 로고
    • Purification and characterization of endoglucanase C from Clostridium cellulolyticum - Catalytic comparison with endoglucanase A
    • Fierobe, H.P., Bagnara-Tardif, C., Gaudin, C., Guerlesquin, F., Sauve, P., Belaich, A. and Belaich, J.P. (1993) Purification and characterization of endoglucanase C from Clostridium cellulolyticum - catalytic comparison with endoglucanase A. Eur. J. Biochem., 217, 557-565.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 557-565
    • Fierobe, H.P.1    Bagnara-Tardif, C.2    Gaudin, C.3    Guerlesquin, F.4    Sauve, P.5    Belaich, A.6    Belaich, J.P.7
  • 30
    • 0030700658 scopus 로고    scopus 로고
    • CelG from Clostridium cellulolyticum: A multidomain endoglucanase acting efficiently on crystalline cellulose
    • Gal, L., Gaudin, C., Belaich, A., Pagès, S., Tardif, C. and Belaich, J.P. (1997a) CelG from Clostridium cellulolyticum: a multidomain endoglucanase acting efficiently on crystalline cellulose. J. Bacteriol., 179, 6595-6601.
    • (1997) J. Bacteriol. , vol.179 , pp. 6595-6601
    • Gal, L.1    Gaudin, C.2    Belaich, A.3    Pagès, S.4    Tardif, C.5    Belaich, J.P.6
  • 32
    • 0025804758 scopus 로고
    • Domains in microbial β-1,4-glycanases: Sequence conservation, function and enzyme families
    • Gilkes, N.R., Henrissat, B., Kilburn, D.G., Miller, R.C., Jr and Warren, A.J. (1991) Domains in microbial β-1,4-glycanases: sequence conservation, function and enzyme families. Microbiol. Rev., 55, 303-315.
    • (1991) Microbiol. Rev. , vol.55 , pp. 303-315
    • Gilkes, N.R.1    Henrissat, B.2    Kilburn, D.G.3    Miller Jr., R.C.4    Warren, A.J.5
  • 33
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in proteins
    • Glusker, J.P. (1991) Structural aspects of metal liganding to functional groups in proteins. Adv. Prot. Chem., 42, 1-76.
    • (1991) Adv. Prot. Chem. , vol.42 , pp. 1-76
    • Glusker, J.P.1
  • 34
    • 0031023626 scopus 로고    scopus 로고
    • A new cellulase family
    • Henrissat, B. (1997) A new cellulase family. Mol. Microbiol., 23, 848-849.
    • (1997) Mol. Microbiol. , vol.23 , pp. 848-849
    • Henrissat, B.1
  • 35
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and Bairoch, A. (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293, 781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 36
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B. and Bairoch, A. (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem. J., 316, 695-696.
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 37
    • 84966185447 scopus 로고
    • Synergism of cellulases from Trichoderma reesei in the degradation of cellulose
    • Henrissat, B., Driguez, H., Viet, C. and Schulein, M. (1985) Synergism of cellulases from Trichoderma reesei in the degradation of cellulose. Biotechnology, 3, 722-726.
    • (1985) Biotechnology , vol.3 , pp. 722-726
    • Henrissat, B.1    Driguez, H.2    Viet, C.3    Schulein, M.4
  • 38
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson, E.G. and Thornton, J.M. (1996) PROMOTIF - a program to identify and analyze structural motifs in proteins. Protein Sci., 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 39
    • 0027651651 scopus 로고
    • Activity studies of eight purified cellulases: Specificity, synergism and binding domain effects
    • Irwin, D.C., Specio, M., Walker, L.P. and Wilson, D.B. (1993) Activity studies of eight purified cellulases: specificity, synergism and binding domain effects. Biotechnol. Bioeng., 42, 1002-1013.
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 1002-1013
    • Irwin, D.C.1    Specio, M.2    Walker, L.P.3    Wilson, D.B.4
  • 40
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penecillopepsion and neuraminidase crystal structures
    • Jiang, J.S. and Brunger, A.T. (1994) Protein hydration observed by X-ray diffraction: solvation properties of penecillopepsion and neuraminidase crystal structures. J. Mol. Biol., 243, 100-115.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brunger, A.T.2
  • 41
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in the models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building models in electron density maps and the location of errors in the models. Acta Crystallogr. Sect. A, 47, 110-119.
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 43
    • 0028229326 scopus 로고
    • Crystal and molecular structure of barley α-amylase
    • Kadziola, A., Abe, J.I., Svensson, B. and Haser, R. (1994) Crystal and molecular structure of barley α-amylase. J. Mol. Biol., 239, 104-121.
    • (1994) J. Mol. Biol. , vol.239 , pp. 104-121
    • Kadziola, A.1    Abe, J.I.2    Svensson, B.3    Haser, R.4
  • 44
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 45
    • 0028901819 scopus 로고
    • Exoglucanase activities of the recombinant Clostridium thermocellum CelS, a major cellulosome component
    • Kruus, K., Wang, W.K., Ching, J. and Wu, J.H. (1995) Exoglucanase activities of the recombinant Clostridium thermocellum CelS, a major cellulosome component. J. Bacteriol., 177, 1641-1644.
    • (1995) J. Bacteriol. , vol.177 , pp. 1641-1644
    • Kruus, K.1    Wang, W.K.2    Ching, J.3    Wu, J.H.4
  • 46
    • 0021016163 scopus 로고
    • Characterization of a cellulose binding cellulase containing complex in Clostridium thermocellum
    • Lamed, R., Setter, E. and Bayer, E.A. (1983) Characterization of a cellulose binding cellulase containing complex in Clostridium thermocellum. J. Bacteriol., 156, 828-836.
    • (1983) J. Bacteriol. , vol.156 , pp. 828-836
    • Lamed, R.1    Setter, E.2    Bayer, E.A.3
  • 47
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., McArthur, N.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    McArthur, N.W.2    Moss, D.S.3    Thornton, J.M.4
  • 48
    • 0026060514 scopus 로고
    • Partial purification and characterization of the cellulases from Clostridium cellulolyticum H10
    • Madarro, E., Pena, J.P. Lequerica, J.L., Vallés, S., Gay, R. and Flors, A. (1991) Partial purification and characterization of the cellulases from Clostridium cellulolyticum H10. J. Chem. Tech. Biotech., 52, 393-406.
    • (1991) J. Chem. Tech. Biotech. , vol.52 , pp. 393-406
    • Madarro, E.1    Pena, J.P.2    Lequerica, J.L.3    Vallés, S.4    Gay, R.5    Flors, A.6
  • 49
  • 50
    • 0028057108 scopus 로고
    • Raster3D version 2.0, a program for photorealistic molecular graphics
    • Merrit, E.A. and Murphy, M.E.P. (1994) Raster3D version 2.0, a program for photorealistic molecular graphics. Acta Crystallogr. Sect. D, 50, 869-837.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 869-1837
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 51
    • 0030902082 scopus 로고    scopus 로고
    • Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from a statistical analysis of saccharide-protein interactions
    • Meyer, J.E.W. and Schulz, G.E. (1997) Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from a statistical analysis of saccharide-protein interactions. Protein Sci., 6, 1084-1091.
    • (1997) Protein Sci. , vol.6 , pp. 1084-1091
    • Meyer, J.E.W.1    Schulz, G.E.2
  • 52
    • 0025879666 scopus 로고
    • Isolation and properties of a major cellobiohydrolase from the cellulosome of Clostridium thermocellum
    • Morag, E., Halevy, I., Bayer, E.A. and Lamed, R. (1991) Isolation and properties of a major cellobiohydrolase from the cellulosome of Clostridium thermocellum. J. Bacteriol., 173, 4155-4162.
    • (1991) J. Bacteriol. , vol.173 , pp. 4155-4162
    • Morag, E.1    Halevy, I.2    Bayer, E.A.3    Lamed, R.4
  • 53
    • 0027133770 scopus 로고
    • Cellulase Ss (CelS) is synonymous with the major cellobiohydrolase (subunit S8) from the cellulosome of Clostridium thermocellum
    • Morag, E., Bayer, E.A., Hazlewood, G.P. Gilbert, H.J. and Lamed, R. (1993) Cellulase Ss (CelS) is synonymous with the major cellobiohydrolase (subunit S8) from the cellulosome of Clostridium thermocellum. Appl. Biochem. Biotechnol., 43, 147-151.
    • (1993) Appl. Biochem. Biotechnol. , vol.43 , pp. 147-151
    • Morag, E.1    Bayer, E.A.2    Hazlewood, G.P.3    Gilbert, H.J.4    Lamed, R.5
  • 55
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet., 11, 282.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 282
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 56
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • Wolf, W., Evans, P.R. and Leslie, A.G.W. (eds), Science and Engineering Research Council, Warrington, UK
    • Otwinowski, Z. (1991) Maximum likelihood refinement of heavy atom parameters. In Wolf, W., Evans, P.R. and Leslie, A.G.W. (eds), Isomorphous Replacement and Anomalous Scattering. Science and Engineering Research Council, Warrington, UK, pp. 80-86.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 57
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer, L., Isaacs, N. and Bailey, S. (eds), Science and Engineering Research Council, Warrington, UK
    • Otwinowski, Z. (1993) Oscillation data reduction program. In Sawyer, L., Isaacs, N. and Bailey, S. (eds), Proceedings of the CCP4 Study Weekend: Data Collection and Processing. Science and Engineering Research Council, Warrington, UK, pp. 56-62.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 58
    • 0029964699 scopus 로고    scopus 로고
    • Interaction between the endoglucanase CelA and the scaffolding protein CipC of the Clostridium cellulolyticum cellulosome
    • Pagès, S., Belaich, A., Tardif, C., Reverbel-Leroy, C., Gaudin, C. and Belaich, J.P. (1996) Interaction between the endoglucanase CelA and the scaffolding protein CipC of the Clostridium cellulolyticum cellulosome. J. Bacteriol., 178, 2279-2286.
    • (1996) J. Bacteriol. , vol.178 , pp. 2279-2286
    • Pagès, S.1    Belaich, A.2    Tardif, C.3    Reverbel-Leroy, C.4    Gaudin, C.5    Belaich, J.P.6
  • 59
    • 0028198814 scopus 로고
    • The active center of a mammalian α-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution
    • Qian, M., Haser, R., Buisson, G., Duée, E. and Payan, F. (1994) The active center of a mammalian α-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution. Biochemistry, 33, 6284-6294.
    • (1994) Biochemistry , vol.33 , pp. 6284-6294
    • Qian, M.1    Haser, R.2    Buisson, G.3    Duée, E.4    Payan, F.5
  • 60
    • 0013815214 scopus 로고
    • Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units
    • Ramakrishnan, C. and Ramachandran, G.N. (1965) Stereochemical criteria for polypeptide and protein chain conformations. II. Allowed conformations for a pair of peptide units. Biophys. J., 5, 909-933.
    • (1965) Biophys. J. , vol.5 , pp. 909-933
    • Ramakrishnan, C.1    Ramachandran, G.N.2
  • 61
    • 0029983647 scopus 로고    scopus 로고
    • Molecular study and overexpression of the Clostridium cellulolyticum celF cellulase gene in Escherichia coli
    • Reverbel-Leroy, C., Belaich, A., Bernadac, A., Gaudin, C., Belaich, J.P. and Tardif, C. (1996) Molecular study and overexpression of the Clostridium cellulolyticum celF cellulase gene in Escherichia coli. Microbiology, 142, 1013-1023.
    • (1996) Microbiology , vol.142 , pp. 1013-1023
    • Reverbel-Leroy, C.1    Belaich, A.2    Bernadac, A.3    Gaudin, C.4    Belaich, J.P.5    Tardif, C.6
  • 62
    • 0031019865 scopus 로고    scopus 로고
    • The processive endocellulase CelF, a major component of the Clostridium cellulolyticum cellulosome. Purification and characterization of the recombinant form
    • Reverbel-Leroy, C., Pagès, S., Belaich, A., Belaich, J.P. and Tardif, C. (1997a) The processive endocellulase CelF, a major component of the Clostridium cellulolyticum cellulosome. Purification and characterization of the recombinant form. J. Bacteriol., 179, 46-52.
    • (1997) J. Bacteriol. , vol.179 , pp. 46-52
    • Reverbel-Leroy, C.1    Pagès, S.2    Belaich, A.3    Belaich, J.P.4    Tardif, C.5
  • 63
    • 0031911214 scopus 로고    scopus 로고
    • Crystallization of the catalytic domain of Clostridium cellulolyticum CelF cellulase in the presence of a newly synthesized cellulase inhibitor
    • Reverbel-Leroy, C. Parsiegla, G., Moreau, V., Juy, M., Tardif, C., Driguez, H., Belaich, J.P. and Haser, R. (1997b) Crystallization of the catalytic domain of Clostridium cellulolyticum CelF cellulase in the presence of a newly synthesized cellulase inhibitor. Acta Crystallogr. Sect. D, 54, 114-118.
    • (1997) Acta Crystallogr. Sect. D , vol.54 , pp. 114-118
    • Reverbel-Leroy, C.1    Parsiegla, G.2    Moreau, V.3    Juy, M.4    Tardif, C.5    Driguez, H.6    Belaich, J.P.7    Haser, R.8
  • 64
    • 0014140609 scopus 로고
    • Multiple attack hypothesis of α-amylase action: Action of porcine pancreatic, human salivary and Aspergillus oryzae α-amylase
    • Robyt, J.F. and French, D. (1967) Multiple attack hypothesis of α-amylase action: action of porcine pancreatic, human salivary and Aspergillus oryzae α-amylase. Arch. Biochem. Biophys, 122, 8-16.
    • (1967) Arch. Biochem. Biophys , vol.122 , pp. 8-16
    • Robyt, J.F.1    French, D.2
  • 65
    • 0025182502 scopus 로고
    • Three dimensional structure of Cellobiohydrolase II from Trichermodenna reesei
    • Rouvinen, J., Bergfors, T., Teeri, T., Knowles, J.K.C. and Jones, T.A. (1990) Three dimensional structure of Cellobiohydrolase II from Trichermodenna reesei. Science, 249, 380-386.
    • (1990) Science , vol.249 , pp. 380-386
    • Rouvinen, J.1    Bergfors, T.2    Teeri, T.3    Knowles, J.K.C.4    Jones, T.A.5
  • 66
    • 0003840108 scopus 로고    scopus 로고
    • Department of NMR Spectroscopy. Bijvoet Center for Biomolecular Reasearch, Utrecht University, The Netherlands
    • Rullmann, J.A.C. (1996) AQUA, computer program. Department of NMR Spectroscopy. Bijvoet Center for Biomolecular Reasearch, Utrecht University, The Netherlands.
    • (1996) AQUA, Computer Program
    • Rullmann, J.A.C.1
  • 67
    • 0026772722 scopus 로고
    • Involvement of separate domains of the cellulosomal protein S1 of Clostridium thermocellum in binding to cellulose and in anchoring of catalytic subunits to the cellulosome
    • Salamitou, S., Tokatlidis, K., Béguin, P. and Aubert, J.P. (1992) Involvement of separate domains of the cellulosomal protein S1 of Clostridium thermocellum in binding to cellulose and in anchoring of catalytic subunits to the cellulosome. FEBS Lett., 304, 89-92.
    • (1992) FEBS Lett. , vol.304 , pp. 89-92
    • Salamitou, S.1    Tokatlidis, K.2    Béguin, P.3    Aubert, J.P.4
  • 68
    • 0030759920 scopus 로고    scopus 로고
    • Structure and mechanism of endo/exocellulase E4 from Thermospora fusca
    • Sakon, J., Irwin, D., Wilson, D.B. and Karplus, P.A. (1997) Structure and mechanism of endo/exocellulase E4 from Thermospora fusca. Nature Struct. Biol., 4, 810-818.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 810-818
    • Sakon, J.1    Irwin, D.2    Wilson, D.B.3    Karplus, P.A.4
  • 70
    • 0025834107 scopus 로고
    • Nucleotide sequence analysis of the endoglucanase-encoding gene, celCCD, of Clostridium cellulolyticum
    • Shima, S., Igararashi, Y. and Kodama, T. (1991) Nucleotide sequence analysis of the endoglucanase-encoding gene, celCCD, of Clostridium cellulolyticum. Gene, 104, 33-38.
    • (1991) Gene , vol.104 , pp. 33-38
    • Shima, S.1    Igararashi, Y.2    Kodama, T.3
  • 71
    • 0027534962 scopus 로고
    • Purification and properties of two truncated endoglucanases produced in Escherichia coli harboring Clostridium cellulolyticum endoglucanase gene celCCD
    • Shima, S., Igrarashi, Y. and Kodama, T. (1993) Purification and properties of two truncated endoglucanases produced in Escherichia coli harboring Clostridium cellulolyticum endoglucanase gene celCCD. Appl. Microbiol. Biotechnol., 38, 750-754.
    • (1993) Appl. Microbiol. Biotechnol. , vol.38 , pp. 750-754
    • Shima, S.1    Igrarashi, Y.2    Kodama, T.3
  • 72
    • 0027385038 scopus 로고
    • Crystal structure of the catalytic domain of a thermophilic endocellulase
    • Spezio, M., Wilson, D.B. and Karplus, P.A. (1993) Crystal structure of the catalytic domain of a thermophilic endocellulase. Biochemistry, 32, 9906-9916.
    • (1993) Biochemistry , vol.32 , pp. 9906-9916
    • Spezio, M.1    Wilson, D.B.2    Karplus, P.A.3
  • 73
    • 0025940435 scopus 로고
    • Interaction of the duplicated segment carried by Clostridium thermocellum cellulases with cellulosome components
    • Tokatlidis, K., Salamitou, S., Béguin, P., Dhurjati, P. and Aubert, J.P. (1991) Interaction of the duplicated segment carried by Clostridium thermocellum cellulases with cellulosome components. FEBS Lett., 291, 185-188.
    • (1991) FEBS Lett. , vol.291 , pp. 185-188
    • Tokatlidis, K.1    Salamitou, S.2    Béguin, P.3    Dhurjati, P.4    Aubert, J.P.5
  • 75
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. (1990) WHAT IF: a molecular modeling and drug design program. J. Mol. Graph., 8, 2577-2637.
    • (1990) J. Mol. Graph. , vol.8 , pp. 2577-2637
    • Vriend, G.1


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