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Volumn 63, Issue 24, 2006, Pages 2954-2967

Recent structural studies of carbohydrate-binding modules

Author keywords

jelly roll fold; sandwich; Carbohydrate binding module; structure and function; Classification; Immunoglobulin fold

Indexed keywords

CARBOHYDRATE; CARBOHYDRATE BINDING PROTEIN; CHITIN; ENZYME; GLUCAN; LIGAND;

EID: 33846113064     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-006-6195-3     Document Type: Review
Times cited : (149)

References (62)
  • 1
    • 0024277381 scopus 로고
    • Studies of the cellulolytic system of Trichoderma reesei QM 9414: Analysis of domain function in two cellobiohydrolases by limited proteolysis
    • Tomme, P., Van Tilbeurgh, H., Pettersson, G., Van Damme, J., Vandekerckhove, J., Knowles, J., Teeri, T. and Claeyssens, M. (1988) Studies of the cellulolytic system of Trichoderma reesei QM 9414: analysis of domain function in two cellobiohydrolases by limited proteolysis. Eur. J. Biochem. 170, 575-581.
    • (1988) Eur. J. Biochem , vol.170 , pp. 575-581
    • Tomme, P.1    Van Tilbeurgh, H.2    Pettersson, G.3    Van Damme, J.4    Vandekerckhove, J.5    Knowles, J.6    Teeri, T.7    Claeyssens, M.8
  • 2
    • 0024297010 scopus 로고
    • Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis
    • Gilkes, N. R., Warren, R. A., Miller, R. C. Jr and Kilburn, D. G. (1988) Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis. J. Biol. Chem. 263, 10401-10407.
    • (1988) J. Biol. Chem , vol.263 , pp. 10401-10407
    • Gilkes, N.R.1    Warren, R.A.2    Miller Jr, R.C.3    Kilburn, D.G.4
  • 5
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • Boraston, A. B., Bolam, D. N., Gilbert, H. J. and Davies, G. J. (2004) Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem. J. 382, 769-781.
    • (2004) Biochem. J , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 6
    • 2342594497 scopus 로고    scopus 로고
    • X-ray crystal structure of a non-crystalline cellulose-specific carbohydrate-binding module: CBM28
    • Jamal, S., Nurizzo, D., Boraston, A. B. and Davies, G. J. (2004) X-ray crystal structure of a non-crystalline cellulose-specific carbohydrate-binding module: CBM28. J. Mol. Biol. 339, 253-258.
    • (2004) J. Mol. Biol , vol.339 , pp. 253-258
    • Jamal, S.1    Nurizzo, D.2    Boraston, A.B.3    Davies, G.J.4
  • 7
    • 0029955959 scopus 로고    scopus 로고
    • Crystal structure of a bacterial family-III cellulose-binding domain: A general mechanism for attachment to cellulose
    • Tormo, J., Lamed, R., Chirino, A. J., Morag, E., Bayer, E. A., Shoham, Y. and Steitz, T. A. (1996) Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J. 15, 5739-5751.
    • (1996) EMBO J , vol.15 , pp. 5739-5751
    • Tormo, J.1    Lamed, R.2    Chirino, A.J.3    Morag, E.4    Bayer, E.A.5    Shoham, Y.6    Steitz, T.A.7
  • 8
    • 0034493730 scopus 로고    scopus 로고
    • Analysis of binding of the family 2a carbohydrate-binding module from Cellulomonas fimi xylanase 10A to cellulose: Specificity and identification of functionally important amino acid residues
    • McLean, B. W., Bray, M. R., Boraston, A. B., Gilkes, N. R., Haynes, C. A. and Kilburn, D. G. (2000) Analysis of binding of the family 2a carbohydrate-binding module from Cellulomonas fimi xylanase 10A to cellulose: specificity and identification of functionally important amino acid residues. Protein Eng. 13, 801-809.
    • (2000) Protein Eng , vol.13 , pp. 801-809
    • McLean, B.W.1    Bray, M.R.2    Boraston, A.B.3    Gilkes, N.R.4    Haynes, C.A.5    Kilburn, D.G.6
  • 9
    • 0032537605 scopus 로고    scopus 로고
    • All three surface tryptophans in Type IIa cellulose binding domains play a pivotal role in binding both soluble and insoluble ligands
    • Nagy, T., Simpson, P., Williamson, M. P., Hazlewood, G. P., Gilbert, H. J. and Orosz, L. (1998) All three surface tryptophans in Type IIa cellulose binding domains play a pivotal role in binding both soluble and insoluble ligands. FEBS Lett. 429, 312-316.
    • (1998) FEBS Lett , vol.429 , pp. 312-316
    • Nagy, T.1    Simpson, P.2    Williamson, M.P.3    Hazlewood, G.P.4    Gilbert, H.J.5    Orosz, L.6
  • 10
    • 0034731387 scopus 로고    scopus 로고
    • The structural basis for the ligand specificity of family 2 carbohydrate-binding modules
    • Simpson, P. J., Xie, H., Bolam, D. N., Gilbert, H. J. and Williamson, M. P. (2000) The structural basis for the ligand specificity of family 2 carbohydrate-binding modules. J. Biol. Chem. 275, 41137-41142.
    • (2000) J. Biol. Chem , vol.275 , pp. 41137-41142
    • Simpson, P.J.1    Xie, H.2    Bolam, D.N.3    Gilbert, H.J.4    Williamson, M.P.5
  • 11
    • 4544354845 scopus 로고    scopus 로고
    • The family II carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates beta-1,4- and beta-1,3-1,4-mixed linked glucans at a single binding site
    • Carvalho, A. L., Goyal, A., Prates, J. A., Bolam, D. N., Gilbert, H. J., Pires, V. M., Ferreira, L. M., Planas, A., Romao, M. J. and Fontes, C. M. (2004) The family II carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates beta-1,4- and beta-1,3-1,4-mixed linked glucans at a single binding site. J. Biol. Chem. 279, 34785-34793.
    • (2004) J. Biol. Chem , vol.279 , pp. 34785-34793
    • Carvalho, A.L.1    Goyal, A.2    Prates, J.A.3    Bolam, D.N.4    Gilbert, H.J.5    Pires, V.M.6    Ferreira, L.M.7    Planas, A.8    Romao, M.J.9    Fontes, C.M.10
  • 12
    • 33644855732 scopus 로고    scopus 로고
    • A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition
    • Boraston, A. B., Healey, M., Klassen, J., Ficko-Blean, E., Lammerts van Bueren, A. and Law, V. (2006) A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition. J. Biol. Chem. 281, 587-598.
    • (2006) J. Biol. Chem , vol.281 , pp. 587-598
    • Boraston, A.B.1    Healey, M.2    Klassen, J.3    Ficko-Blean, E.4    Lammerts van Bueren, A.5    Law, V.6
  • 14
    • 23644454654 scopus 로고    scopus 로고
    • The first crystal structure of a family 31 carbohydrate-binding module with affinity to beta-1,3-xylan
    • Hashimoto, H., Tamai, Y., Okazaki, F., Tamaru, Y., Shimizu, T., Araki, T. and Sato, M. (2005) The first crystal structure of a family 31 carbohydrate-binding module with affinity to beta-1,3-xylan. FEBS Lett. 579, 4324-4328.
    • (2005) FEBS Lett , vol.579 , pp. 4324-4328
    • Hashimoto, H.1    Tamai, Y.2    Okazaki, F.3    Tamaru, Y.4    Shimizu, T.5    Araki, T.6    Sato, M.7
  • 15
    • 15744367514 scopus 로고    scopus 로고
    • Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21
    • Vaaje-Kolstad, G., Houston, D. R., Riemen, A. H., Eijsink, V. G. and van Aalten, D. M. (2005) Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21. J. Biol. Chem. 280, 11313-11319.
    • (2005) J. Biol. Chem , vol.280 , pp. 11313-11319
    • Vaaje-Kolstad, G.1    Houston, D.R.2    Riemen, A.H.3    Eijsink, V.G.4    van Aalten, D.M.5
  • 16
    • 14644407391 scopus 로고    scopus 로고
    • Structure of a mannan-specific family 35 carbohydrate-binding module: Evidence for significant conformational changes upon ligand binding
    • Tunnicliffe, R. B., Bolam, D. N., Pell, G., Gilbert, H. J. and Williamson, M. P. (2005) Structure of a mannan-specific family 35 carbohydrate-binding module: evidence for significant conformational changes upon ligand binding. J. Mol. Biol. 347, 287-296.
    • (2005) J. Mol. Biol , vol.347 , pp. 287-296
    • Tunnicliffe, R.B.1    Bolam, D.N.2    Pell, G.3    Gilbert, H.J.4    Williamson, M.P.5
  • 17
    • 7244254401 scopus 로고    scopus 로고
    • Crystal structure of a family 54 alpha-L- arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose
    • Miyanaga, A., Koseki, T., Matsuzawa, H., Wakagi, T., Shoun, H. and Fushinobu, S. (2004) Crystal structure of a family 54 alpha-L- arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose. J. Biol. Chem. 279, 44907-44914.
    • (2004) J. Biol. Chem , vol.279 , pp. 44907-44914
    • Miyanaga, A.1    Koseki, T.2    Matsuzawa, H.3    Wakagi, T.4    Shoun, H.5    Fushinobu, S.6
  • 18
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 19
    • 0035824881 scopus 로고    scopus 로고
    • Recognition of cello-oligosaccharides by a family 17 carbohydrate-binding module: An X-ray crystallographic, thermodynamic and mutagenic study
    • Notenboom, V., Boraston, A. B., Chiu, P., Freelove, A. C., Kilburn, D. G. and Rose, D. R. (2001) Recognition of cello-oligosaccharides by a family 17 carbohydrate-binding module: an X-ray crystallographic, thermodynamic and mutagenic study. J. Mol. Biol. 314, 797-806.
    • (2001) J. Mol. Biol , vol.314 , pp. 797-806
    • Notenboom, V.1    Boraston, A.B.2    Chiu, P.3    Freelove, A.C.4    Kilburn, D.G.5    Rose, D.R.6
  • 21
    • 2542453684 scopus 로고    scopus 로고
    • X4 modules represent a new family of carbohydrate-binding modules that display novel properties
    • Bolam, D. N., Xie, H., Pell, G., Hogg, D., Galbraith, G., Henrissat, B. and Gilbert, H. J. (2004) X4 modules represent a new family of carbohydrate-binding modules that display novel properties. J. Biol. Chem. 279, 22953-22963.
    • (2004) J. Biol. Chem , vol.279 , pp. 22953-22963
    • Bolam, D.N.1    Xie, H.2    Pell, G.3    Hogg, D.4    Galbraith, G.5    Henrissat, B.6    Gilbert, H.J.7
  • 22
    • 2442709187 scopus 로고    scopus 로고
    • The crystal structure of the family 6 carbohydrate binding module from Cellvibrio mixtus endoglucanase 5a in complex with oligosaccharides reveals two distinct binding sites with different ligand specificities
    • Pires, V. M., Henshaw, J. L., Prates, J. A., Bolam, D. N., Ferreira, L. M., Fontes, C. M., Henrissat, B., Planas, A., Gilbert, H. J. and Czjzek, M. (2004) The crystal structure of the family 6 carbohydrate binding module from Cellvibrio mixtus endoglucanase 5a in complex with oligosaccharides reveals two distinct binding sites with different ligand specificities. J. Biol. Chem. 279, 21560-21568.
    • (2004) J. Biol. Chem , vol.279 , pp. 21560-21568
    • Pires, V.M.1    Henshaw, J.L.2    Prates, J.A.3    Bolam, D.N.4    Ferreira, L.M.5    Fontes, C.M.6    Henrissat, B.7    Planas, A.8    Gilbert, H.J.9    Czjzek, M.10
  • 23
    • 2442681858 scopus 로고    scopus 로고
    • The family 6 carbohydrate binding module CmCBM6-2 contains two ligand-binding sites with distinct specificities
    • Henshaw, J. L., Bolam, D. N., Pires, V. M., Czjzek, M., Henrissat, B., Ferreira, L. M., Fontes, C. M. and Gilbert, H. J. (2004) The family 6 carbohydrate binding module CmCBM6-2 contains two ligand-binding sites with distinct specificities. J. Biol. Chem. 279, 21552-21559.
    • (2004) J. Biol. Chem , vol.279 , pp. 21552-21559
    • Henshaw, J.L.1    Bolam, D.N.2    Pires, V.M.3    Czjzek, M.4    Henrissat, B.5    Ferreira, L.M.6    Fontes, C.M.7    Gilbert, H.J.8
  • 24
    • 0029820612 scopus 로고    scopus 로고
    • Cloning, DNA sequencing, and expression of the gene encoding Clostridium thermocellum cellulase CelJ, the largest catalytic component of the cellulosome
    • Ahsan, M. M., Kimura, T., Karita, S., Sakka, K. and Ohmiya, K. (1996) Cloning, DNA sequencing, and expression of the gene encoding Clostridium thermocellum cellulase CelJ, the largest catalytic component of the cellulosome. J. Bacteriol. 178, 5732-5740.
    • (1996) J. Bacteriol , vol.178 , pp. 5732-5740
    • Ahsan, M.M.1    Kimura, T.2    Karita, S.3    Sakka, K.4    Ohmiya, K.5
  • 25
    • 0037226350 scopus 로고    scopus 로고
    • Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: Importance of the CBM to cellulose hydrolysis
    • Arai, T., Araki, R., Tanaka, A., Karita, S., Kimura, T., Sakka, K. and Ohmiya, K. (2003) Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: importance of the CBM to cellulose hydrolysis. J. Bacteriol. 185, 504-512.
    • (2003) J. Bacteriol , vol.185 , pp. 504-512
    • Arai, T.1    Araki, R.2    Tanaka, A.3    Karita, S.4    Kimura, T.5    Sakka, K.6    Ohmiya, K.7
  • 26
    • 3142576945 scopus 로고    scopus 로고
    • Ab initio structure determination and functional characterization of CBM36; a new family of calcium-dependent carbohydrate binding modules
    • Jamal-Talabani, S., Boraston, A. B., Turkenburg, J. P., Tarbouriech, N., Ducros, V. M. and Davies, G. J. (2004) Ab initio structure determination and functional characterization of CBM36; a new family of calcium-dependent carbohydrate binding modules. Structure 12, 1177-1187.
    • (2004) Structure , vol.12 , pp. 1177-1187
    • Jamal-Talabani, S.1    Boraston, A.B.2    Turkenburg, J.P.3    Tarbouriech, N.4    Ducros, V.M.5    Davies, G.J.6
  • 27
    • 0033555277 scopus 로고    scopus 로고
    • The structure of a PKD domain from polycystin-1: Implications for polycystic kidney disease
    • Bycroft, M., Bateman, A., Clarke, J., Hamill, S. J., Sandford, R., Thomas, R. L. and Chothia, C. (1999) The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease. EMBO J. 18, 297-305.
    • (1999) EMBO J , vol.18 , pp. 297-305
    • Bycroft, M.1    Bateman, A.2    Clarke, J.3    Hamill, S.J.4    Sandford, R.5    Thomas, R.L.6    Chothia, C.7
  • 29
    • 0031662792 scopus 로고    scopus 로고
    • Purification and substrate specificities of two alpha-L- arabinofuranosidases from Aspergillus awamori IFO 4033
    • Kaneko, S., Arimoto, M., Ohba, M., Kobayashi, H., Ishii, T. and Kusakabe, I. (1998) Purification and substrate specificities of two alpha-L- arabinofuranosidases from Aspergillus awamori IFO 4033. Appl. Environ. Microbiol. 64, 4021-4027.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 4021-4027
    • Kaneko, S.1    Arimoto, M.2    Ohba, M.3    Kobayashi, H.4    Ishii, T.5    Kusakabe, I.6
  • 30
    • 0034253281 scopus 로고    scopus 로고
    • Alpha-L-arabinofuranosidases: Biochemistry, molecular biology and application in biotechnology
    • Saha, B. C. (2000) Alpha-L-arabinofuranosidases: biochemistry, molecular biology and application in biotechnology. Biotechnol. Adv. 18, 403-423.
    • (2000) Biotechnol. Adv , vol.18 , pp. 403-423
    • Saha, B.C.1
  • 31
    • 0141888400 scopus 로고    scopus 로고
    • Role of two alpha-L-arabinofuranosidases in arabinoxylan degradation and characteristics of the encoding genes from shochu koji molds, Aspergillus kawachii and Aspergillus awamori
    • Koseki, T., Okuda, M., Sudoh, S., Kizaki, Y., Iwano, K., Aramaki, I. and Matsuzawa, H. (2003) Role of two alpha-L-arabinofuranosidases in arabinoxylan degradation and characteristics of the encoding genes from shochu koji molds, Aspergillus kawachii and Aspergillus awamori. J. Biosci. Bioeng. 96, 232-241.
    • (2003) J. Biosci. Bioeng , vol.96 , pp. 232-241
    • Koseki, T.1    Okuda, M.2    Sudoh, S.3    Kizaki, Y.4    Iwano, K.5    Aramaki, I.6    Matsuzawa, H.7
  • 32
    • 0033991365 scopus 로고    scopus 로고
    • An alpha-L-arabinofuranosidase from Penicillium purpurogenum: Production, purification and properties
    • De Ioannes, P., Peirano, A., Steiner, J. and Eyzaguirre, J. (2000) An alpha-L-arabinofuranosidase from Penicillium purpurogenum: production, purification and properties. J. Biotechnol. 76, 253-258.
    • (2000) J. Biotechnol , vol.76 , pp. 253-258
    • De Ioannes, P.1    Peirano, A.2    Steiner, J.3    Eyzaguirre, J.4
  • 33
    • 17644434949 scopus 로고    scopus 로고
    • Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase
    • Hovel, K., Shallom, D., Niefind, K., Belakhov, V., Shoham, G., Baasov, T., Shoham, Y. and Schomburg, D. (2003) Crystal structure and snapshots along the reaction pathway of a family 51 alpha-L-arabinofuranosidase. EMBO J. 22, 4922-4932.
    • (2003) EMBO J , vol.22 , pp. 4922-4932
    • Hovel, K.1    Shallom, D.2    Niefind, K.3    Belakhov, V.4    Shoham, G.5    Baasov, T.6    Shoham, Y.7    Schomburg, D.8
  • 34
    • 0037070548 scopus 로고    scopus 로고
    • The identification of the acid-base catalyst of alpha-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase
    • Shallom, D., Belakhov, V., Solomon, D., Gilead-Gropper, S., Baasov, T., Shoham, G. and Shoham, Y. (2002) The identification of the acid-base catalyst of alpha-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase. FEBS Lett. 514, 163-167.
    • (2002) FEBS Lett , vol.514 , pp. 163-167
    • Shallom, D.1    Belakhov, V.2    Solomon, D.3    Gilead-Gropper, S.4    Baasov, T.5    Shoham, G.6    Shoham, Y.7
  • 35
    • 0346319022 scopus 로고    scopus 로고
    • Detailed kinetic analysis and identification of the nucleophile in alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase
    • Shallom, D., Belakhov, V., Solomon, D., Shoham, G., Baasov, T. and Shoham, Y. (2002) Detailed kinetic analysis and identification of the nucleophile in alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase. J. Biol. Chem. 277, 43667-43673.
    • (2002) J. Biol. Chem , vol.277 , pp. 43667-43673
    • Shallom, D.1    Belakhov, V.2    Solomon, D.3    Shoham, G.4    Baasov, T.5    Shoham, Y.6
  • 36
    • 0032486273 scopus 로고    scopus 로고
    • Novel galactose-binding proteins in Annelida: Characterization of 29-kDa tandem repeat-type lectins from the earthworm Lumbricus terrestris
    • Hirabayashi, J., Dutta, S. K. and Kasai, K. (1998) Novel galactose-binding proteins in Annelida: characterization of 29-kDa tandem repeat-type lectins from the earthworm Lumbricus terrestris. J. Biol. Chem. 273, 14450-14460.
    • (1998) J. Biol. Chem , vol.273 , pp. 14450-14460
    • Hirabayashi, J.1    Dutta, S.K.2    Kasai, K.3
  • 38
    • 0036300580 scopus 로고    scopus 로고
    • Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: Sugar binding structure of the family 13 carbohydrate binding module
    • Fujimoto, Z., Kuno, A., Kaneko, S., Kobayashi, H., Kusakabe, I. and Mizuno, H. (2002) Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module. J. Mol. Biol. 316, 65-78.
    • (2002) J. Mol. Biol , vol.316 , pp. 65-78
    • Fujimoto, Z.1    Kuno, A.2    Kaneko, S.3    Kobayashi, H.4    Kusakabe, I.5    Mizuno, H.6
  • 39
    • 1542274526 scopus 로고    scopus 로고
    • Crystal structures of decorated xylooligosaccharides bound to a family 10 xylanase from Streptomyces olivaceoviridis E-86
    • Fujimoto, Z., Kaneko, S., Kuno, A., Kobayashi, H., Kusakabe, I. and Mizuno, H. (2004) Crystal structures of decorated xylooligosaccharides bound to a family 10 xylanase from Streptomyces olivaceoviridis E-86. J. Biol. Chem. 279, 9606-9614.
    • (2004) J. Biol. Chem , vol.279 , pp. 9606-9614
    • Fujimoto, Z.1    Kaneko, S.2    Kuno, A.3    Kobayashi, H.4    Kusakabe, I.5    Mizuno, H.6
  • 40
    • 0037006986 scopus 로고    scopus 로고
    • High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding
    • Notenboom, V., Boraston, A. B., Williams, S. J., Kilburn, D. G. and Rose, D. R. (2002) High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding. Biochemistry 41, 4246-4254.
    • (2002) Biochemistry , vol.41 , pp. 4246-4254
    • Notenboom, V.1    Boraston, A.B.2    Williams, S.J.3    Kilburn, D.G.4    Rose, D.R.5
  • 42
    • 0027932706 scopus 로고
    • Thermodynamics of ligand binding to the starch-binding domain of glucoamylase from Aspergillus niger
    • Sigurskjold, B. W., Svensson, B., Williamson, G. and Driguez, H. (1994) Thermodynamics of ligand binding to the starch-binding domain of glucoamylase from Aspergillus niger. Eur. J. Biochem. 225, 133-141.
    • (1994) Eur. J. Biochem , vol.225 , pp. 133-141
    • Sigurskjold, B.W.1    Svensson, B.2    Williamson, G.3    Driguez, H.4
  • 43
    • 0031570348 scopus 로고    scopus 로고
    • Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin
    • Sorimachi, K., Le Gal-Coeffet, M. F., Williamson, G., Archer, D. B. and Williamson, M. P. (1997) Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin. Structure 5, 647-661.
    • (1997) Structure , vol.5 , pp. 647-661
    • Sorimachi, K.1    Le Gal-Coeffet, M.F.2    Williamson, G.3    Archer, D.B.4    Williamson, M.P.5
  • 44
    • 0035834494 scopus 로고    scopus 로고
    • Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose
    • Giardina, T., Gunning, A. P., Juge, N., Faulds, C. B., Furniss, C. S., Svensson, B., Morris, V. J. and Williamson, G. (2001) Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose. J. Mol. Biol. 313, 1149-1159.
    • (2001) J. Mol. Biol , vol.313 , pp. 1149-1159
    • Giardina, T.1    Gunning, A.P.2    Juge, N.3    Faulds, C.B.4    Furniss, C.S.5    Svensson, B.6    Morris, V.J.7    Williamson, G.8
  • 45
  • 46
    • 10644283902 scopus 로고    scopus 로고
    • Alpha-glucan recognition by a new family of carbohydrate-binding modules found primarily in bacterial pathogens
    • Lammerts van Bueren, A., Finn, R., Ausio, J. and Boraston, A.B. (2004) Alpha-glucan recognition by a new family of carbohydrate-binding modules found primarily in bacterial pathogens. Biochemistry 43, 15633-15642.
    • (2004) Biochemistry , vol.43 , pp. 15633-15642
    • Lammerts van Bueren, A.1    Finn, R.2    Ausio, J.3    Boraston, A.B.4
  • 47
    • 0030604713 scopus 로고    scopus 로고
    • Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy
    • Sorimachi, K., Jacks, A. J., Le Gal-Coeffet, M. F., Williamson, G., Archer, D. B. and Williamson, M. P. (1996) Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 259, 970-987.
    • (1996) J. Mol. Biol , vol.259 , pp. 970-987
    • Sorimachi, K.1    Jacks, A.J.2    Le Gal-Coeffet, M.F.3    Williamson, G.4    Archer, D.B.5    Williamson, M.P.6
  • 48
    • 1542495429 scopus 로고    scopus 로고
    • Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain
    • Abe, A., Tonozuka, T., Sakano, Y. and Kamitori, S. (2004) Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain. J. Mol. Biol. 335, 811-822.
    • (2004) J. Mol. Biol , vol.335 , pp. 811-822
    • Abe, A.1    Tonozuka, T.2    Sakano, Y.3    Kamitori, S.4
  • 50
    • 0036192464 scopus 로고    scopus 로고
    • Co-operative binding of triplicate carbohydrate-binding modules from a thermophilic xylanase
    • Boraston, A. B., McLean, B. W., Chen, G., Li, A., Warren, R. A. and Kilburn, D. G. (2002) Co-operative binding of triplicate carbohydrate-binding modules from a thermophilic xylanase. Mol. Microbiol. 43, 187-194.
    • (2002) Mol. Microbiol , vol.43 , pp. 187-194
    • Boraston, A.B.1    McLean, B.W.2    Chen, G.3    Li, A.4    Warren, R.A.5    Kilburn, D.G.6
  • 51
    • 0035957081 scopus 로고    scopus 로고
    • Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A
    • Bolam, D. N., Xie, H., White, P., Simpson, P. J., Hancock, S. M., Williamson, M. P. and Gilbert, H. J. (2001) Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A. Biochemistry 40, 2468-2477.
    • (2001) Biochemistry , vol.40 , pp. 2468-2477
    • Bolam, D.N.1    Xie, H.2    White, P.3    Simpson, P.J.4    Hancock, S.M.5    Williamson, M.P.6    Gilbert, H.J.7
  • 52
    • 0036226314 scopus 로고    scopus 로고
    • Novel carbohydrate-binding module of beta-1,3-xylanase from a marine bacterium, Alcaligenes sp. strain XY-234
    • Okazaki, F., Tamaru, Y., Hashikawa, S., Li, Y. T. and Araki, T. (2002) Novel carbohydrate-binding module of beta-1,3-xylanase from a marine bacterium, Alcaligenes sp. strain XY-234. J. Bacteriol. 184, 2399-2403.
    • (2002) J. Bacteriol , vol.184 , pp. 2399-2403
    • Okazaki, F.1    Tamaru, Y.2    Hashikawa, S.3    Li, Y.T.4    Araki, T.5
  • 53
    • 0033574502 scopus 로고    scopus 로고
    • Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution
    • Kamitori, S., Kondo, S., Okuyama, K., Yokota, T., Shimura, Y., Tonozuka, T. and Sakano, Y. (1999) Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution. J. Mol. Biol. 287, 907-921.
    • (1999) J. Mol. Biol , vol.287 , pp. 907-921
    • Kamitori, S.1    Kondo, S.2    Okuyama, K.3    Yokota, T.4    Shimura, Y.5    Tonozuka, T.6    Sakano, Y.7
  • 54
    • 0035967536 scopus 로고    scopus 로고
    • Crystal structures of the family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10A in native and ligand-bound forms
    • Notenboom, V., Boraston, A. B., Kilburn, D. G. and Rose, D. R. (2001) Crystal structures of the family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10A in native and ligand-bound forms. Biochemistry 40, 6248-6256.
    • (2001) Biochemistry , vol.40 , pp. 6248-6256
    • Notenboom, V.1    Boraston, A.B.2    Kilburn, D.G.3    Rose, D.R.4
  • 55
    • 0034127684 scopus 로고    scopus 로고
    • Expression and characterization of the chitin-binding domain of chitinase A1 from Bacillus circulons WL-12
    • Hashimoto, M., Ikegami, T., Seino, S., Ohuchi, N., Fukada, H., Sugiyama, J., Shirakawa, M. and Watanabe, T. (2000) Expression and characterization of the chitin-binding domain of chitinase A1 from Bacillus circulons WL-12. J. Bacteriol. 182, 3045-3054.
    • (2000) J. Bacteriol , vol.182 , pp. 3045-3054
    • Hashimoto, M.1    Ikegami, T.2    Seino, S.3    Ohuchi, N.4    Fukada, H.5    Sugiyama, J.6    Shirakawa, M.7    Watanabe, T.8
  • 56
    • 0034674709 scopus 로고    scopus 로고
    • Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif
    • Suetake, T., Tsuda, S., Kawabata, S., Miura, K., Iwanaga, S., Hikichi, K., Nitta, K. and Kawano, K. (2000) Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif. J. Biol. Chem. 275, 17929-17932.
    • (2000) J. Biol. Chem , vol.275 , pp. 17929-17932
    • Suetake, T.1    Tsuda, S.2    Kawabata, S.3    Miura, K.4    Iwanaga, S.5    Hikichi, K.6    Nitta, K.7    Kawano, K.8
  • 57
    • 0034609570 scopus 로고    scopus 로고
    • Solution structure and conformational changes of the Streptomyces chitin-binding protein (CHB1)
    • Svergun, D. I., Becirevic, A., Schrempf, H., Koch, M. H. and Gruber, G. (2000) Solution structure and conformational changes of the Streptomyces chitin-binding protein (CHB1). Biochemistry 39, 10677-10683.
    • (2000) Biochemistry , vol.39 , pp. 10677-10683
    • Svergun, D.I.1    Becirevic, A.2    Schrempf, H.3    Koch, M.H.4    Gruber, G.5
  • 58
    • 0031602025 scopus 로고    scopus 로고
    • Chitin binding protein (CBP21) in the culture supernatant of Serratia marcescens 2170
    • Suzuki, K., Suzuki, M., Taiyoji, M., Nikaidou, N. and Watanabe, T. (1998) Chitin binding protein (CBP21) in the culture supernatant of Serratia marcescens 2170. Biosci. Biotechnol. Biochem. 62, 128-135.
    • (1998) Biosci. Biotechnol. Biochem , vol.62 , pp. 128-135
    • Suzuki, K.1    Suzuki, M.2    Taiyoji, M.3    Nikaidou, N.4    Watanabe, T.5
  • 59
    • 0030958337 scopus 로고    scopus 로고
    • Specific interaction of the Streptomyces chitin-binding protein CHB1 with alpha-chitin - the role of individual tryptophan residues
    • Zeltins, A. and Schrempf, H. (1997) Specific interaction of the Streptomyces chitin-binding protein CHB1 with alpha-chitin - the role of individual tryptophan residues. Eur. J. Biochem. 246, 557-564.
    • (1997) Eur. J. Biochem , vol.246 , pp. 557-564
    • Zeltins, A.1    Schrempf, H.2
  • 60
    • 27644529698 scopus 로고    scopus 로고
    • A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21
    • Machovic, M., Svensson, B., MacGregor, E. A. and Janecek, S. (2005) A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21. FEBS J. 272, 5497-5513.
    • (2005) FEBS J , vol.272 , pp. 5497-5513
    • Machovic, M.1    Svensson, B.2    MacGregor, E.A.3    Janecek, S.4
  • 61
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (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.1
  • 62
    • 0028057108 scopus 로고    scopus 로고
    • Merritt, E. A. and Murphy, M. E, 1994 Raster3D Version 2.0: a program for photorealistic molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 50, 869-873
    • Merritt, E. A. and Murphy, M. E. (1994) Raster3D Version 2.0: a program for photorealistic molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 50, 869-873.


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