메뉴 건너뛰기




Volumn 272, Issue 3, 1997, Pages 383-397

The crystal structure of the catalytic core domain of endoglucanase I from trichoderma reesei at 3.6 Å resolution, and a comparison with related enzymes

Author keywords

Cellulase; Cellulose; Endoglucanase; Protein structure; X ray crystallography

Indexed keywords

CELLULOSE; CELLULOSE 1,4 BETA CELLOBIOSIDASE; FUNGAL PROTEIN; GLUCAN SYNTHASE; GLYCOSIDASE;

EID: 0031587296     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1243     Document Type: Article
Times cited : (223)

References (76)
  • 2
    • 0021668869 scopus 로고
    • Isolation of celluloytic enzymes from Trichoderma reesei QM 9414
    • Bhikhabai R., Johansson G., Petterson G. Isolation of celluloytic enzymes from Trichoderma reesei QM 9414. J. Appl. Biochem. 6:1984;336-345.
    • (1984) J. Appl. Biochem. , vol.6 , pp. 336-345
    • Bhikhabai, R.1    Johansson, G.2    Petterson, G.3
  • 3
    • 0019869086 scopus 로고
    • Substrate-binding site of endo-1,4-β-xylanase of the yeast Cryptococcus albidus
    • Biely P., Krátky Z., Vrsanská M. Substrate-binding site of endo-1,4-β-xylanase of the yeast Cryptococcus albidus. Eur. J. Biochem. 119:1991a;559-564.
    • (1991) Eur. J. Biochem. , vol.119 , pp. 559-564
    • Biely, P.1    Krátky, Z.2    Vrsanská, M.3
  • 4
    • 0025908702 scopus 로고
    • The endo-1,4-β-glucanase I from Trichoderna reesei. Action on β-1,4-oligomers and polyerms derived from D -glucose and D -xylose
    • Biely P., Vrsanska M., Claeyssens M. The endo-1,4-β-glucanase I from Trichoderna reesei. Action on β-1,4-oligomers and polyerms derived from D -glucose and D -xylose. Eur. J. Biochem. 200:1991b;157-163.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 157-163
    • Biely, P.1    Vrsanska, M.2    Claeyssens, M.3
  • 5
    • 0040930710 scopus 로고
    • Mode of action of Trichoderma reeseiβ-1,4-glucanases on cellooligosaccharides
    • Foundation for Biotechnical and Industrial Fermentation Research, Helsinki
    • Biely P., Vrsanska M., Claeyssens M. Mode of action of Trichoderma reeseiβ-1,4-glucanases on cellooligosaccharides. Trichoderma reesei Cellulases and Other Hydrolases. 1993;Foundation for Biotechnical and Industrial Fermentation Research, Helsinki.
    • (1993) Trichoderma Reesei Cellulases and Other Hydrolases
    • Biely, P.1    Vrsanska, M.2    Claeyssens, M.3
  • 7
    • 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. 335:1992;472-475.
    • (1992) Nature , vol.335 , pp. 472-475
    • Brünger, A.T.1
  • 8
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger A. T, Kuriyan J., Karplus M. Crystallographic R factor refinement by molecular dynamics. Science. 235:1987;458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 9
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brünger A. T, Krukowski A., Erickson J. Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallog. sect. A. 46:1990;585-593.
    • (1990) Acta Crystallog. Sect. A , vol.46 , pp. 585-593
    • Brünger, A.T.1    Krukowski, A.2    Erickson, J.3
  • 10
    • 0027051606 scopus 로고
    • Specificity mapping of cellulolytic enzymes: Classification into families of structurally related proteins confirmed by biochemical analysis
    • Claeyssens M., Henrissat B. Specificity mapping of cellulolytic enzymes: classification into families of structurally related proteins confirmed by biochemical analysis. Protein Sci. 1:1992;1293-1297.
    • (1992) Protein Sci. , vol.1 , pp. 1293-1297
    • Claeyssens, M.1    Henrissat, B.2
  • 12
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 13
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure. 3:1995;853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 15
    • 0003690659 scopus 로고
    • Acta Universitatis Upsaliensis. Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology Uppsala University, Uppsala, Sweden
    • Divne, C. 1994, The three-dimensional structure of cellobiohydrolase I from Trichoderma reesei Acta Universitatis Upsaliensis. Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, vol. 47, Uppsala University, Uppsala, Sweden.
    • (1994) The Three-dimensional Structure of Cellobiohydrolase I from Trichoderma Reesei , vol.47
    • Divne, C.1
  • 20
  • 22
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R. A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A. 47:1991;392-400.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 23
    • 0016275528 scopus 로고
    • The structure of native cellulose
    • Gardner K. H., Blackwell J. The structure of native cellulose. Biopolymers. 13:1974;1975-2001.
    • (1974) Biopolymers , vol.13 , pp. 1975-2001
    • Gardner, K.H.1    Blackwell, J.2
  • 24
    • 0028812262 scopus 로고
    • Crystal structure and site- directed mutagenesis of Bacillus macerans endo-1, 3-1,4-β-glucanase
    • Hahn M., Olsen O., Politz O., Borriss R., Heinemann U. Crystal structure and site- directed mutagenesis of Bacillus macerans endo-1, 3-1,4-β-glucanase. J. Biol. Chem. 270:1995;3081-3088.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3081-3088
    • Hahn, M.1    Olsen, O.2    Politz, O.3    Borriss, R.4    Heinemann, U.5
  • 25
    • 0015516458 scopus 로고
    • Structure of concanavalin A at 2.4-Å resolution
    • Haradman K. D., Ainsworth C. F. Structure of concanavalin A at 2.4-Å resolution. Biochemistry. 11:1972;4910-4919.
    • (1972) Biochemistry , vol.11 , pp. 4910-4919
    • Haradman, K.D.1    Ainsworth, C.F.2
  • 26
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280:1991;309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 27
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B., Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293:1993;781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 28
    • 84966185447 scopus 로고
    • Synergism of cellulases from Trichoderma reesei in the degradation of cellulose
    • Henrissat B., Driguez H., Viet C., Schülein M. Synergism of cellulases from Trichoderma reesei in the degradation of cellulose. Bio/Technology. 3:1985;722-726.
    • (1985) Bio/Technology , vol.3 , pp. 722-726
    • Henrissat, B.1    Driguez, H.2    Viet, C.3    Schülein, M.4
  • 30
    • 0003450992 scopus 로고
    • New York: Academic Press
    • International Union of Biochemistry and Molecular Biology. Enzyme Nomenclature. 1992;Academic Press, New York.
    • (1992) Enzyme Nomenclature
  • 31
    • 0022701772 scopus 로고
    • Using known substructures in protein model building and crystallography
    • Jones T. A., Thirup S. Using known substructures in protein model building and crystallography. EMBO J. 5:1986;819-822.
    • (1986) EMBO J. , vol.5 , pp. 819-822
    • Jones, T.A.1    Thirup, S.2
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 34
    • 0027161796 scopus 로고
    • Molecular and active-site structure of a Bacillus 1,3-1,4-β-glucanase
    • Keitel T., Simon O., Borriss R., Heinemann U. Molecular and active-site structure of a Bacillus 1,3-1,4-β-glucanase. Proc. Natl Acad. Sci. USA. 90:1993;5287-5291.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5287-5291
    • Keitel, T.1    Simon, O.2    Borriss, R.3    Heinemann, U.4
  • 35
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • Kleywegt G. J. Use of non-crystallographic symmetry in protein structure refinement. Acta Crystallog. sect. D. 52:1996;842-857.
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 842-857
    • Kleywegt, G.J.1
  • 36
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination: Applications of the free R value
    • Kleywegt G. J., Brünger A. T. Checking your imagination: applications of the free R value. Structure. 4:1996;897-904.
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brünger, A.T.2
  • 37
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt G. J., Jones T. A. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallog. sect. D. 50:1994a;178-185.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 38
    • 0002700643 scopus 로고
    • Halloween ... masks and bones
    • S. Bailey, R. Hubbard, & D.A. Waller. Warrington: SERC Daresbury Laboratory
    • Kleywegt G. J., Jones T. A. Halloween ... masks and bones. Bailey S., Hubbard R., Waller D. A. From First Map to Final Model. 1994b;SERC Daresbury Laboratory, Warrington.
    • (1994) From First Map to Final Model
    • Kleywegt, G.J.1    Jones, T.A.2
  • 39
    • 0008840364 scopus 로고
    • Braille for pugilists
    • W.N. Hunter, J.M. Thornton, & S. Bailey. Warrington: SERC Daresbury Laboratory
    • Kleywegt G. J., Jones T. A. Braille for pugilists. Hunter W. N., Thornton J. M., Bailey S. Making the Most of Your Model. 1995a;SERC Daresbury Laboratory, Warrington.
    • (1995) Making the Most of Your Model
    • Kleywegt, G.J.1    Jones, T.A.2
  • 40
    • 0029644940 scopus 로고
    • Where freedom is given, liberties are taken
    • Kleywegt G. J., Jones T. A. Where freedom is given, liberties are taken. Structure. 3:1995b;535-540.
    • (1995) Structure , vol.3 , pp. 535-540
    • Kleywegt, G.J.1    Jones, T.A.2
  • 41
    • 0030497978 scopus 로고    scopus 로고
    • Efficient rebuilding of protein structures
    • Kleywegt G. J., Jones T. A. Efficient rebuilding of protein structures. Acta Crystallog. sect. D. 52:1996a;829-832.
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 829-832
    • Kleywegt, G.J.1    Jones, T.A.2
  • 42
    • 0030589514 scopus 로고    scopus 로고
    • Phi/psi-chology: Ramachandran revisited
    • Kleywegt G. J., Jones T. A. Phi/psi-chology: Ramachandran revisited. Structure. 4:1996b;1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 43
    • 0030845843 scopus 로고    scopus 로고
    • Model-building and refinement practice
    • Kleywegt G. J., Jones T. A. Model-building and refinement practice. Methods Enzymol. 277:1997;in the press.
    • (1997) Methods Enzymol , vol.277
    • Kleywegt, G.J.1    Jones, T.A.2
  • 44
    • 0028774713 scopus 로고
    • Crystal structures of cellular retinoic acid binding proteins I and II in complex with all- trans -retinoic acid and a synthetic retinoid
    • Kleywegt G. J., Bergfors T., Senn H., Le Motte P., Gsell B., Shudo K., Jones T. A. Crystal structures of cellular retinoic acid binding proteins I and II in complex with all- trans -retinoic acid and a synthetic retinoid. Structure. 2:1994;1241-1258.
    • (1994) Structure , vol.2 , pp. 1241-1258
    • Kleywegt, G.J.1    Bergfors, T.2    Senn, H.3    Le Motte, P.4    Gsell, B.5    Shudo, K.6    Jones, T.A.7
  • 45
    • 0025043403 scopus 로고
    • Quantification of the main components of the Trichoderma cellulose complex with monoclonal antibodies using an enzyme-linked immunosorbent assay (ELISA)
    • Kolbe J., Kubicek C. P. Quantification of the main components of the Trichoderma cellulose complex with monoclonal antibodies using an enzyme-linked immunosorbent assay (ELISA). Appl. Microbiol. Biotechnol. 34:1990;26-30.
    • (1990) Appl. Microbiol. Biotechnol. , vol.34 , pp. 26-30
    • Kolbe, J.1    Kubicek, C.P.2
  • 46
    • 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. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 47
    • 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 P. J., Clore G. M., Nilges M., Jones T. A., Pettersson G., Knowles J., Gronenborn A. M. 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. 28:1989;7241-7257.
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, P.J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 48
    • 0011241750 scopus 로고
    • Evaluation of protein coordinate sets
    • S. Bailey, R. Hubbard, & D.A. Waller. Warrington: SERC Daresbury Laboratory
    • Laskowski R. A., MacArthur M. W., Thornton J. M. Evaluation of protein coordinate sets. Bailey S., Hubbard R., Waller D. A. From First Map to Final Model. 1994;SERC Daresbury Laboratory, Warrington.
    • (1994) From First Map to Final Model
    • Laskowski, R.A.1    MacArthur, M.W.2    Thornton, J.M.3
  • 49
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la détermination des structures cristallines
    • Luzzati V. Traitement statistique des erreurs dans la détermination des structures cristallines. Acta Crystallog. 5:1952;802-810.
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 50
    • 0030947305 scopus 로고    scopus 로고
    • Identification of the catalytic nucleophile of endoglucanase I from Fusarium oxysporum by mass spectrometry
    • MacKenzie L., Davies G. J., Schülein M., Withers S. G. Identification of the catalytic nucleophile of endoglucanase I from Fusarium oxysporum by mass spectrometry. Biochemistry. 36:1997;5893-5901.
    • (1997) Biochemistry , vol.36 , pp. 5893-5901
    • MacKenzie, L.1    Davies, G.J.2    Schülein, M.3    Withers, S.G.4
  • 51
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B. W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 54
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 55
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowsk Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowsk, Z.1    Minor, W.2
  • 56
    • 0022969096 scopus 로고
    • Homology between cellulase genes of Trichoderma reesei: Complete nucleotide sequence of the endoglucanase I gene
    • Penttilä M., Lehtovaara P., Nevalainen H., Bhikhabhai R., Knowles J. Homology between cellulase genes of Trichoderma reesei: complete nucleotide sequence of the endoglucanase I gene. Gene. 45:1986;253-263.
    • (1986) Gene , vol.45 , pp. 253-263
    • Penttilä, M.1    Lehtovaara, P.2    Nevalainen, H.3    Bhikhabhai, R.4    Knowles, J.5
  • 57
    • 0023155210 scopus 로고
    • Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder J. W., Richards F. M. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193:1987;775-791.
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 58
    • 0013815214 scopus 로고
    • Stereochemical criteria for polypeptide and protein chain conformation. II. Allowed conformations for a pair of peptide units
    • Ramakrishnan C., Ramachandran G. N. Stereochemical criteria for polypeptide and protein chain conformation. II. Allowed conformations for a pair of peptide units. Biophys. J. 5:1965;909-933.
    • (1965) Biophys. J. , vol.5 , pp. 909-933
    • Ramakrishnan, C.1    Ramachandran, G.N.2
  • 59
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • Rice L. M., Brünger A. T. Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement. Proteins: Struct. Funct. Genet. 19:1994;277-290.
    • (1994) Proteins: Struct. Funct. Genet. , vol.19 , pp. 277-290
    • Rice, L.M.1    Brünger, A.T.2
  • 61
    • 0002660809 scopus 로고
    • The detection of sub-units within the crystallographic asymmetric unit
    • Rossmann M. G., Blow D. M. The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallog. 15:1962;24-31.
    • (1962) Acta Crystallog. , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Blow, D.M.2
  • 62
    • 0025182502 scopus 로고
    • Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei
    • Rouvinen J., Bergfors T., Teeri T., Knowles J. K. C., Jones T. A. Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. Science. 249:1990;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
  • 63
    • 0027381121 scopus 로고
    • Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases
    • Schou C., Rasmussen G., Kaltoft M.-B., Henrissat B., Schülein M. Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases. Eur. J. Biochem. 217:1993;947-953.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 947-953
    • Schou, C.1    Rasmussen, G.2    Kaltoft, M.-B.3    Henrissat, B.4    Schülein, M.5
  • 64
    • 0040848319 scopus 로고
    • Humicola insolens alkaline cellulases
    • P. Suominen, & T. Reinikainen. Foundation for Biotechnical and Industrial Fermentation Research, Helsinki
    • Schülein M., Tikhomirov D. F., Schou C. Humicola insolens alkaline cellulases. Suominen P., Reinikainen T. Trichoderma reesei Cellulases and other Hydrolases. 1993;Foundation for Biotechnical and Industrial Fermentation Research, Helsinki.
    • (1993) Trichoderma Reesei Cellulases and other Hydrolases
    • Schülein, M.1    Tikhomirov, D.F.2    Schou, C.3
  • 65
    • 0027385038 scopus 로고
    • Crystal structure of the catalytic domain of a thermophilic endocellulase
    • Spezio M. L., Wilson D. B., Karplus P. A. Crystal structure of the catalytic domain of a thermophilic endocellulase. Biochemistry. 32:1993;9906-9916.
    • (1993) Biochemistry , vol.32 , pp. 9906-9916
    • Spezio, M.L.1    Wilson, D.B.2    Karplus, P.A.3
  • 66
    • 0030606294 scopus 로고    scopus 로고
    • Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesi
    • Ståhlberg J., Divne C., Koivula A., Piens K., Claeyssens M., Teeri T. T., Jones T. A. Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesi. J. Mol. Biol. 264:1996;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
  • 67
    • 0029856409 scopus 로고    scopus 로고
    • Structure of the Fusarium oxysporum endoglucanase I with a non-hydrolysable substrate analogue: Substrate distortion gives rise to a pseudo-axial orientation for the leaving group
    • Sulzenbacher G., Driguez H., Henrissat B., Schülein M., Davies G. J. Structure of the Fusarium oxysporum endoglucanase I with a non-hydrolysable substrate analogue: substrate distortion gives rise to a pseudo-axial orientation for the leaving group. Biochemistry. 35:1996;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
  • 68
    • 0343488512 scopus 로고    scopus 로고
    • Structures of the endoglucanase I from Fusarium oxysporum: Native, cellobiose and 3,4-epoxybutyl β- D -cellobioside inhibited forms at 2.3 Å resolution
    • Sulzenbacher G., Schülein M., Davies G. J. Structures of the endoglucanase I from Fusarium oxysporum: native, cellobiose and 3,4-epoxybutyl β- D -cellobioside inhibited forms at 2.3 Å resolution. Biochemistry. 36:1997;5902-5911.
    • (1997) Biochemistry , vol.36 , pp. 5902-5911
    • Sulzenbacher, G.1    Schülein, M.2    Davies, G.J.3
  • 69
    • 0023132478 scopus 로고
    • Homologous domains in Tricholderma reesei cellulolytic enzymes: Gene sequence and expression of cellobiohydrolase II
    • Teeri T., Lehtovaara P., Kauppinen S., Salovuori I., Knowles J. K. C. Homologous domains in Tricholderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II. Gene. 51:1987;43-52.
    • (1987) Gene , vol.51 , pp. 43-52
    • Teeri, T.1    Lehtovaara, P.2    Kauppinen, S.3    Salovuori, I.4    Knowles, J.K.C.5
  • 70
  • 71
    • 0028911057 scopus 로고
    • Structural comparison of two major endo -1,4-xylanases from Trichoderma reesei
    • Törrönen A., Rouvinen J. Structural comparison of two major endo -1,4-xylanases from Trichoderma reesei. Biochemistry. 34:1995;847-856.
    • (1995) Biochemistry , vol.34 , pp. 847-856
    • Törrönen, A.1    Rouvinen, J.2
  • 72
    • 0028338985 scopus 로고
    • Three-dimensional structure of endo-1,4-β-xylanase II from Trichoderma reesei: Two conformational states in the active site
    • Törrönen A., Harkki A., Rouvinen J. Three-dimensional structure of endo-1,4-β-xylanase II from Trichoderma reesei: two conformational states in the active site. EMBO J. 13:1994;2493-2501.
    • (1994) EMBO J. , vol.13 , pp. 2493-2501
    • Törrönen, A.1    Harkki, A.2    Rouvinen, J.3
  • 74
    • 0027542118 scopus 로고
    • Quality control of protein models: Directional atomic contact analysis
    • Vriend G., Sander C. Quality control of protein models: directional atomic contact analysis. J. Appl. Crystallog. 26:1993;47-60.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 47-60
    • Vriend, G.1    Sander, C.2
  • 75
    • 0027943686 scopus 로고
    • Crystal structure of the catalytic domain of the β-1,4-glycanase Cex from Cellulomonas fimi
    • White A., Withers S. G., Gilkes N. R., Rose D. R. Crystal structure of the catalytic domain of the β-1,4-glycanase Cex from Cellulomonas fimi. Biochemistry. 33:1994;12546-12552.
    • (1994) Biochemistry , vol.33 , pp. 12546-12552
    • White, A.1    Withers, S.G.2    Gilkes, N.R.3    Rose, D.R.4
  • 76
    • 0028039323 scopus 로고
    • An evaluation of the use of databases in protein structure refinement
    • Zou J. Y., Mowbray S. L. An evaluation of the use of databases in protein structure refinement. Acta Crystallog. sect. D. 50:1994;237-249.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 237-249
    • Zou, J.Y.1    Mowbray, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.