메뉴 건너뛰기




Volumn 23, Issue 5, 2013, Pages 669-677

Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydrate-binding modules

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; CHITIN; CHITINASE; GLYCAN; GLYCOSIDE; HYDROLASE; POLYSACCHARIDE; POLYSACCHARIDE LYASE;

EID: 84885472019     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2013.05.005     Document Type: Review
Times cited : (276)

References (54)
  • 3
    • 77953219138 scopus 로고    scopus 로고
    • The biochemistry and structural biology of plant cell wall deconstruction
    • Gilbert H.J. The biochemistry and structural biology of plant cell wall deconstruction. Plant Physiol 2010, 153:444-455.
    • (2010) Plant Physiol , vol.153 , pp. 444-455
    • Gilbert, H.J.1
  • 4
    • 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., Claeyssens M. Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis. Eur J Biochem 1988, 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
  • 5
    • 77956988940 scopus 로고    scopus 로고
    • Carbohydrate-binding modules promote the enzymatic deconstruction of intact plant cell walls by targeting and proximity effects
    • Herve C., Rogowski A., Blake A.W., Marcus S.E., Gilbert H.J., Knox J.P. Carbohydrate-binding modules promote the enzymatic deconstruction of intact plant cell walls by targeting and proximity effects. Proc Natl Acad Sci U S A 2010, 107:15293-15298.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 15293-15298
    • Herve, C.1    Rogowski, A.2    Blake, A.W.3    Marcus, S.E.4    Gilbert, H.J.5    Knox, J.P.6
  • 7
    • 23344446196 scopus 로고    scopus 로고
    • The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation
    • Vaaje-Kolstad G., Horn S.J., van Aalten D.M., Synstad B., Eijsink V.G. The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. J Biol Chem 2005, 280:28492-28497.
    • (2005) J Biol Chem , vol.280 , pp. 28492-28497
    • Vaaje-Kolstad, G.1    Horn, S.J.2    van Aalten, D.M.3    Synstad, B.4    Eijsink, V.G.5
  • 11
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: fine-tuning polysaccharide recognition
    • Boraston A.B., Bolam D.N., Gilbert H.J., Davies G.J. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J 2004, 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
  • 12
    • 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 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 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
  • 13
    • 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., Steitz T.A. Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J 1996, 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
  • 15
    • 84866279744 scopus 로고    scopus 로고
    • Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin
    • Georgelis N., Yennawar N.H., Cosgrove D.J. Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin. Proc Natl Acad Sci U S A 2012, 109:14830-14835.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 14830-14835
    • Georgelis, N.1    Yennawar, N.H.2    Cosgrove, D.J.3
  • 16
    • 0036300988 scopus 로고    scopus 로고
    • Differential oligosaccharide recognition by evolutionarily-related beta-1,4 and beta-1,3 glucan-binding modules
    • Boraston A.B., Nurizzo D., Notenboom V., Ducros V., Rose D.R., Kilburn D.G., Davies G.J. Differential oligosaccharide recognition by evolutionarily-related beta-1,4 and beta-1,3 glucan-binding modules. J Mol Biol 2002, 319:1143-1156.
    • (2002) J Mol Biol , vol.319 , pp. 1143-1156
    • Boraston, A.B.1    Nurizzo, D.2    Notenboom, V.3    Ducros, V.4    Rose, D.R.5    Kilburn, D.G.6    Davies, G.J.7
  • 17
    • 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., Rose D.R. Recognition of cello-oligosaccharides by a family 17 carbohydrate-binding module: an X-ray crystallographic, thermodynamic and mutagenic study. J Mol Biol 2001, 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
  • 18
    • 0037195075 scopus 로고    scopus 로고
    • Promiscuity in ligand-binding: the three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose
    • Charnock S.J., Bolam D.N., Nurizzo D., Szabo L., McKie V.A., Gilbert H.J., Davies G.J. Promiscuity in ligand-binding: the three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose. Proc Natl Acad Sci U S A 2002, 99:14077-14082.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 14077-14082
    • Charnock, S.J.1    Bolam, D.N.2    Nurizzo, D.3    Szabo, L.4    McKie, V.A.5    Gilbert, H.J.6    Davies, G.J.7
  • 19
    • 0029965579 scopus 로고    scopus 로고
    • Binding of the cellulose-binding domain of exoglucanase Cex from Cellulomonas fimi to insoluble microcrystalline cellulose is entropically driven
    • Creagh A.L., Ong E., Jervis E., Kilburn D.G., Haynes C.A. Binding of the cellulose-binding domain of exoglucanase Cex from Cellulomonas fimi to insoluble microcrystalline cellulose is entropically driven. Proc Natl Acad Sci U S A 1996, 93:12229-12234.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 12229-12234
    • Creagh, A.L.1    Ong, E.2    Jervis, E.3    Kilburn, D.G.4    Haynes, C.A.5
  • 20
    • 0030825785 scopus 로고    scopus 로고
    • Surface diffusion of cellulases and their isolated binding domains on cellulose
    • Jervis E.J., Haynes C.A., Kilburn D.G. 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
  • 22
    • 0025791694 scopus 로고
    • Conformational properties of beta-(1-]4)-d-galactan determined from chiroptical measurements
    • Duda C.A., Stevens E.S., Reid J.S.G. Conformational properties of beta-(1-]4)-d-galactan determined from chiroptical measurements. Macromolecules 1991, 24:431-435.
    • (1991) Macromolecules , vol.24 , pp. 431-435
    • Duda, C.A.1    Stevens, E.S.2    Reid, J.S.G.3
  • 23
    • 66149188138 scopus 로고    scopus 로고
    • Investigating the binding of beta-1,4-galactan to Bacillus licheniformis beta-1,4-galactanase by crystallography and computational modeling
    • Le Nours J., De Maria L., Welner D., Jorgensen C.T., Christensen L.L., Borchert T.V., Larsen S., Lo Leggio L. Investigating the binding of beta-1,4-galactan to Bacillus licheniformis beta-1,4-galactanase by crystallography and computational modeling. Proteins 2009, 75:977-989.
    • (2009) Proteins , vol.75 , pp. 977-989
    • Le Nours, J.1    De Maria, L.2    Welner, D.3    Jorgensen, C.T.4    Christensen, L.L.5    Borchert, T.V.6    Larsen, S.7    Lo Leggio, L.8
  • 24
    • 78149267267 scopus 로고    scopus 로고
    • Recognition of the helical structure of beta-1,4-galactan by a new family of carbohydrate-binding modules
    • Cid M., Pedersen H.L., Kaneko S., Coutinho P.M., Henrissat B., Willats W.G., Boraston A.B. Recognition of the helical structure of beta-1,4-galactan by a new family of carbohydrate-binding modules. J Biol Chem 2010, 285:35999-36009.
    • (2010) J Biol Chem , vol.285 , pp. 35999-36009
    • Cid, M.1    Pedersen, H.L.2    Kaneko, S.3    Coutinho, P.M.4    Henrissat, B.5    Willats, W.G.6    Boraston, A.B.7
  • 26
    • 0142134866 scopus 로고    scopus 로고
    • Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate binding module, TmCBM27
    • Boraston A.B., Revett T.J., Boraston C.M., Nurizzo D., Davies G.J. Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate binding module, TmCBM27. Structure (Camb) 2003, 11:665-675.
    • (2003) Structure (Camb) , vol.11 , pp. 665-675
    • Boraston, A.B.1    Revett, T.J.2    Boraston, C.M.3    Nurizzo, D.4    Davies, G.J.5
  • 30
    • 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., Davies G.J. Ab initio structure determination and functional characterization of CBM36; a new family of calcium-dependent carbohydrate binding modules. Structure 2004, 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
  • 33
    • 79959362561 scopus 로고    scopus 로고
    • A novel, noncatalytic carbohydrate-binding module displays specificity for galactose-containing polysaccharides through calcium-mediated oligomerization
    • Montanier C.Y., Correia M.A., Flint J.E., Zhu Y., Basle A., McKee L.S., Prates J.A., Polizzi S.J., Coutinho P.M., Lewis R.J., et al. A novel, noncatalytic carbohydrate-binding module displays specificity for galactose-containing polysaccharides through calcium-mediated oligomerization. J Biol Chem 2011, 286:22499-22509.
    • (2011) J Biol Chem , vol.286 , pp. 22499-22509
    • Montanier, C.Y.1    Correia, M.A.2    Flint, J.E.3    Zhu, Y.4    Basle, A.5    McKee, L.S.6    Prates, J.A.7    Polizzi, S.J.8    Coutinho, P.M.9    Lewis, R.J.10
  • 36
    • 57349113816 scopus 로고    scopus 로고
    • Cell surface enzyme attachment is mediated by family 37 carbohydrate-binding modules, unique to Ruminococcus albus
    • Ezer A., Matalon E., Jindou S., Borovok I., Atamna N., Yu Z., Morrison M., Bayer E.A., Lamed R. Cell surface enzyme attachment is mediated by family 37 carbohydrate-binding modules, unique to Ruminococcus albus. J Bacteriol 2008, 190:8220-8222.
    • (2008) J Bacteriol , vol.190 , pp. 8220-8222
    • Ezer, A.1    Matalon, E.2    Jindou, S.3    Borovok, I.4    Atamna, N.5    Yu, Z.6    Morrison, M.7    Bayer, E.A.8    Lamed, R.9
  • 38
    • 84876889073 scopus 로고    scopus 로고
    • The structure of a Streptomyces avermitilis alpha-l-rhamnosidase reveals a novel carbohydrate-binding module CBM67 within the six-domain arrangement
    • Fujimoto Z., Jackson A., Michikawa M., Maehara T., Momma M., Henrissat B., Gilbert H.J., Kaneko S. The structure of a Streptomyces avermitilis alpha-l-rhamnosidase reveals a novel carbohydrate-binding module CBM67 within the six-domain arrangement. J Biol Chem 2013, 288.
    • (2013) J Biol Chem , vol.288
    • Fujimoto, Z.1    Jackson, A.2    Michikawa, M.3    Maehara, T.4    Momma, M.5    Henrissat, B.6    Gilbert, H.J.7    Kaneko, S.8
  • 40
    • 0000178351 scopus 로고    scopus 로고
    • A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity
    • Simpson P.J., Bolam D.N., Cooper A., Ciruela A., Hazlewood G.P., Gilbert H.J., Williamson M.P. A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity. Structure 1999, 7:853-864.
    • (1999) Structure , vol.7 , pp. 853-864
    • Simpson, P.J.1    Bolam, D.N.2    Cooper, A.3    Ciruela, A.4    Hazlewood, G.P.5    Gilbert, H.J.6    Williamson, M.P.7
  • 41
    • 0035966110 scopus 로고    scopus 로고
    • Structure of a family 15 carbohydrate-binding module in complex with xylopentaose. Evidence that xylan binds in an approximate 3-fold helical conformation
    • Szabo L., Jamal S., Xie H., Charnock S.J., Bolam D.N., Gilbert H.J., Davies G.J. Structure of a family 15 carbohydrate-binding module in complex with xylopentaose. Evidence that xylan binds in an approximate 3-fold helical conformation. J Biol Chem 2001, 276:49061-49065.
    • (2001) J Biol Chem , vol.276 , pp. 49061-49065
    • Szabo, L.1    Jamal, S.2    Xie, H.3    Charnock, S.J.4    Bolam, D.N.5    Gilbert, H.J.6    Davies, G.J.7
  • 43
    • 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., Czjzek M. 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 2004, 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
  • 44
    • 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., Rose D.R. Crystal structures of the family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10A in native and ligand-bound forms. Biochemistry 2001, 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
  • 45
    • 0345701247 scopus 로고    scopus 로고
    • Structure and ligand binding of carbohydrate-binding module CsCBM6-3 reveals similarities with fucose-specific lectins and "galactose-binding" domains
    • Boraston A.B., Notenboom V., Warren R.A., Kilburn D.G., Rose D.R., Davies G. Structure and ligand binding of carbohydrate-binding module CsCBM6-3 reveals similarities with fucose-specific lectins and "galactose-binding" domains. J Mol Biol 2003, 327:659-669.
    • (2003) J Mol Biol , vol.327 , pp. 659-669
    • Boraston, A.B.1    Notenboom, V.2    Warren, R.A.3    Kilburn, D.G.4    Rose, D.R.5    Davies, G.6
  • 46
    • 33749394275 scopus 로고    scopus 로고
    • Understanding the biological rationale for the diversity of cellulose-directed carbohydrate-binding modules in prokaryotic enzymes
    • Blake A.W., McCartney L., Flint J.E., Bolam D.N., Boraston A.B., Gilbert H.J., Knox J.P. Understanding the biological rationale for the diversity of cellulose-directed carbohydrate-binding modules in prokaryotic enzymes. J Biol Chem 2006, 281:29321-29329.
    • (2006) J Biol Chem , vol.281 , pp. 29321-29329
    • Blake, A.W.1    McCartney, L.2    Flint, J.E.3    Bolam, D.N.4    Boraston, A.B.5    Gilbert, H.J.6    Knox, J.P.7
  • 47
    • 0034641715 scopus 로고    scopus 로고
    • Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose
    • Carrard G., Koivula A., Soderlund H., Beguin P. Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose. Proc Natl Acad Sci U S A 2000, 97:10342-10347.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10342-10347
    • Carrard, G.1    Koivula, A.2    Soderlund, H.3    Beguin, P.4
  • 51
    • 84873021244 scopus 로고    scopus 로고
    • The carbohydrate-binding module of xylanase from Nonomuraea flexuosa decreases its non-productive adsorption on lignin
    • Zhang J.H., Moilanen U., Tang M., Viikari L. The carbohydrate-binding module of xylanase from Nonomuraea flexuosa decreases its non-productive adsorption on lignin. Biotechnol Biofuels 2013, 6.
    • (2013) Biotechnol Biofuels , pp. 6
    • Zhang, J.H.1    Moilanen, U.2    Tang, M.3    Viikari, L.4
  • 52
    • 84871896986 scopus 로고    scopus 로고
    • Imaging and measuring single-molecule interaction between a carbohydrate-binding module and natural plant cell wall cellulose
    • Zhang M., Wu S.-C., Zhou W., Xu B. Imaging and measuring single-molecule interaction between a carbohydrate-binding module and natural plant cell wall cellulose. J Phys Chem B 2012, 116:9949-9956.
    • (2012) J Phys Chem B , vol.116 , pp. 9949-9956
    • Zhang, M.1    Wu, S.-C.2    Zhou, W.3    Xu, B.4
  • 54
    • 12844253112 scopus 로고    scopus 로고
    • Family 6 carbohydrate binding modules recognize the non-reducing end of beta-1,3-linked glucans by presenting a unique ligand binding surface
    • Lammerts van Bueren A.L., Morland C., Gilbert H.J., Boraston A.B. Family 6 carbohydrate binding modules recognize the non-reducing end of beta-1,3-linked glucans by presenting a unique ligand binding surface. J Biol Chem 2005, 280:530-537.
    • (2005) J Biol Chem , vol.280 , pp. 530-537
    • Lammerts van Bueren, A.L.1    Morland, C.2    Gilbert, H.J.3    Boraston, A.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.