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Volumn 28, Issue 1, 2014, Pages 32-40

Using structure to inform carbohydrate binding module function

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CARBOHYDRATE; CARBOHYDRATE ACTIVE ENZYME; CARBOHYDRATE BINDING MODULE; ENZYME; STARCH; UNCLASSIFIED DRUG; PROTEIN; PROTEIN BINDING;

EID: 84905381472     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2014.07.004     Document Type: Review
Times cited : (89)

References (57)
  • 1
    • 84867745280 scopus 로고    scopus 로고
    • Insights into the recognition of the human glycome by microbial carbohydrate-binding modules
    • Ficko-Blean E., Boraston A.B. Insights into the recognition of the human glycome by microbial carbohydrate-binding modules. Curr Opin Struct Biol 2012, 22:570-577.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 570-577
    • Ficko-Blean, E.1    Boraston, A.B.2
  • 2
    • 84885472019 scopus 로고    scopus 로고
    • Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydrate-binding modules
    • Gilbert H.J., Knox J.P., Boraston A.B. Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydrate-binding modules. Curr Opin Struct Biol 2013, 23:669-677.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 669-677
    • Gilbert, H.J.1    Knox, J.P.2    Boraston, A.B.3
  • 3
    • 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
  • 4
    • 33847696168 scopus 로고    scopus 로고
    • Identification and characterization of a novel periplasmic polygalacturonic acid binding protein from Yersinia enterolitica
    • Abbott D.W., Hrynuik S., Boraston A.B. Identification and characterization of a novel periplasmic polygalacturonic acid binding protein from Yersinia enterolitica. J Mol Biol 2007, 367:1023-1033.
    • (2007) J Mol Biol , vol.367 , pp. 1023-1033
    • Abbott, D.W.1    Hrynuik, S.2    Boraston, A.B.3
  • 6
    • 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
  • 8
    • 84864008607 scopus 로고    scopus 로고
    • Two unique ligand-binding clamps of Rhizopus oryzae starch binding domain for helical structure disruption of amylose
    • Jiang T.Y., Ci Y.P., Chou W.I., Lee Y.C., Sun Y.J., Chou W.Y., Li K.M., Chang M.D. Two unique ligand-binding clamps of Rhizopus oryzae starch binding domain for helical structure disruption of amylose. PLoS ONE 2012, 7:e41131.
    • (2012) PLoS ONE , vol.7
    • Jiang, T.Y.1    Ci, Y.P.2    Chou, W.I.3    Lee, Y.C.4    Sun, Y.J.5    Chou, W.Y.6    Li, K.M.7    Chang, M.D.8
  • 9
    • 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., Kamitori S. 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 2004, 335:811-822.
    • (2004) J Mol Biol , vol.335 , pp. 811-822
    • Abe, A.1    Tonozuka, T.2    Sakano, Y.3    Kamitori, S.4
  • 10
    • 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., Williamson G. Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose. J Mol Biol 2001, 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
  • 11
    • 84861138884 scopus 로고    scopus 로고
    • Quantitative approaches to the analysis of carbohydrate-binding module function
    • Abbott D.W., Boraston A.B. Quantitative approaches to the analysis of carbohydrate-binding module function. Methods Enzymol 2012, 510:211-231.
    • (2012) Methods Enzymol , vol.510 , pp. 211-231
    • Abbott, D.W.1    Boraston, A.B.2
  • 12
    • 33846096051 scopus 로고    scopus 로고
    • Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors
    • van Bueren A.L., Higgins M., Wang D., Burke R.D., Boraston A.B. Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors. Nat Struct Mol Biol 2007, 14:76-84.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 76-84
    • van Bueren, A.L.1    Higgins, M.2    Wang, D.3    Burke, R.D.4    Boraston, A.B.5
  • 13
    • 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
  • 17
    • 38349101110 scopus 로고    scopus 로고
    • Insight into ligand diversity and novel biological roles for family 32 carbohydrate-binding modules
    • Abbott D.W., Eirin-Lopez J.M., Boraston A.B. Insight into ligand diversity and novel biological roles for family 32 carbohydrate-binding modules. Mol Biol Evol 2008, 25:155-167.
    • (2008) Mol Biol Evol , vol.25 , pp. 155-167
    • Abbott, D.W.1    Eirin-Lopez, J.M.2    Boraston, A.B.3
  • 20
    • 45549100630 scopus 로고    scopus 로고
    • Divergent modes of glycan recognition by a new family of carbohydrate-binding modules
    • Gregg K.J., Finn R., Abbott D.W., Boraston A.B. Divergent modes of glycan recognition by a new family of carbohydrate-binding modules. J Biol Chem 2008, 283:12604-12613.
    • (2008) J Biol Chem , vol.283 , pp. 12604-12613
    • Gregg, K.J.1    Finn, R.2    Abbott, D.W.3    Boraston, A.B.4
  • 21
    • 80054683038 scopus 로고    scopus 로고
    • Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals
    • Janecek S., Svensson B., MacGregor E.A. Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals. Enzyme Microb Technol 2011, 49:429-440.
    • (2011) Enzyme Microb Technol , vol.49 , pp. 429-440
    • Janecek, S.1    Svensson, B.2    MacGregor, E.A.3
  • 22
    • 84894116866 scopus 로고    scopus 로고
    • Fine-structural variance of family 3 carbohydrate-binding modules as extracellular biomass-sensing components of Clostridium thermocellum anti-sigmaI factors
    • Yaniv O., Fichman G., Borovok I., Shoham Y., Bayer E.A., Lamed R., Shimon L.J., Frolow F. Fine-structural variance of family 3 carbohydrate-binding modules as extracellular biomass-sensing components of Clostridium thermocellum anti-sigmaI factors. Acta Crystallogr D Biol Crystallogr 2014, 70:522-534.
    • (2014) Acta Crystallogr D Biol Crystallogr , vol.70 , pp. 522-534
    • Yaniv, O.1    Fichman, G.2    Borovok, I.3    Shoham, Y.4    Bayer, E.A.5    Lamed, R.6    Shimon, L.J.7    Frolow, F.8
  • 23
    • 84871697209 scopus 로고    scopus 로고
    • Reconstruction of ancestral metabolic enzymes reveals molecular mechanisms underlying evolutionary innovation through gene duplication
    • Voordeckers K., Brown C.A., Vanneste K., van der Zande E., Voet A., Maere S., Verstrepen K.J. Reconstruction of ancestral metabolic enzymes reveals molecular mechanisms underlying evolutionary innovation through gene duplication. PLoS Biol 2012, 10:e1001446.
    • (2012) PLoS Biol , vol.10
    • Voordeckers, K.1    Brown, C.A.2    Vanneste, K.3    van der Zande, E.4    Voet, A.5    Maere, S.6    Verstrepen, K.J.7
  • 24
    • 0033797419 scopus 로고    scopus 로고
    • Sugar-lectin interactions: sugar clusters, lectin multivalency and avidity
    • Monsigny M., Mayer R., Roche A.C. Sugar-lectin interactions: sugar clusters, lectin multivalency and avidity. Carbohydr Lett 2000, 4:35-52.
    • (2000) Carbohydr Lett , vol.4 , pp. 35-52
    • Monsigny, M.1    Mayer, R.2    Roche, A.C.3
  • 25
    • 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., Gilbert H.J. X4 modules represent a new family of carbohydrate-binding modules that display novel properties. J Biol Chem 2004, 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
  • 26
    • 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., Williamson M.P. Structure of a mannan-specific family 35 carbohydrate-binding module: evidence for significant conformational changes upon ligand binding. J Mol Biol 2005, 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
  • 31
    • 65649151773 scopus 로고    scopus 로고
    • Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens
    • Ficko-Blean E., Gregg K.J., Adams J.J., Hehemann J.H., Czjzek M., Smith S.P., Boraston A.B. Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens. J Biol Chemist 2009, 284:9876-9884.
    • (2009) J Biol Chemist , vol.284 , pp. 9876-9884
    • Ficko-Blean, E.1    Gregg, K.J.2    Adams, J.J.3    Hehemann, J.H.4    Czjzek, M.5    Smith, S.P.6    Boraston, A.B.7
  • 32
    • 84880661396 scopus 로고    scopus 로고
    • Structure of the Streptococcus pneumoniae surface protein and adhesin PfbA
    • Suits M.D., Boraston A.B. Structure of the Streptococcus pneumoniae surface protein and adhesin PfbA. PLOS ONE 2013, 8:e67190.
    • (2013) PLOS ONE , vol.8
    • Suits, M.D.1    Boraston, A.B.2
  • 33
    • 84861180864 scopus 로고    scopus 로고
    • Small-angle X-ray scattering and crystallography: a winning combination for exploring the multimodular organization of cellulolytic macromolecular complexes
    • Czjzek M., Fierobe H.P., Receveur-Brechot V. Small-angle X-ray scattering and crystallography: a winning combination for exploring the multimodular organization of cellulolytic macromolecular complexes. Methods Enzymol 2012, 510:183-210.
    • (2012) Methods Enzymol , vol.510 , pp. 183-210
    • Czjzek, M.1    Fierobe, H.P.2    Receveur-Brechot, V.3
  • 34
    • 80051665526 scopus 로고    scopus 로고
    • The overall architecture and receptor binding of pneumococcal carbohydrate-antigen-hydrolyzing enzymes
    • Higgins M.A., Ficko-Blean E., Meloncelli P.J., Lowary T.L., Boraston A.B. The overall architecture and receptor binding of pneumococcal carbohydrate-antigen-hydrolyzing enzymes. J Mol Biol 2011, 411:1017-1036.
    • (2011) J Mol Biol , vol.411 , pp. 1017-1036
    • Higgins, M.A.1    Ficko-Blean, E.2    Meloncelli, P.J.3    Lowary, T.L.4    Boraston, A.B.5
  • 36
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley L.A., Sternberg M.J. Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 2009, 4:363-371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 37
    • 3242887695 scopus 로고    scopus 로고
    • Protein structure prediction and analysis using the Robetta server
    • Kim D.E., Chivian D., Baker D. Protein structure prediction and analysis using the Robetta server. Nucleic Acids Res 2004, 32:W526-W531.
    • (2004) Nucleic Acids Res , vol.32
    • Kim, D.E.1    Chivian, D.2    Baker, D.3
  • 38
    • 67349191450 scopus 로고    scopus 로고
    • N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH
    • Ficko-Blean E., Boraston A.B. N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH. J Mol Biol 2009, 390:208-220.
    • (2009) J Mol Biol , vol.390 , pp. 208-220
    • Ficko-Blean, E.1    Boraston, A.B.2
  • 39
    • 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
  • 41
    • 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
  • 42
    • 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
  • 43
    • 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
  • 44
    • 78049395091 scopus 로고    scopus 로고
    • Mutational insights into the roles of amino acid residues in ligand binding for two closely related family 16 carbohydrate binding modules
    • Su X., Agarwal V., Dodd D., Bae B., Mackie R.I., Nair S.K., Cann I.K. Mutational insights into the roles of amino acid residues in ligand binding for two closely related family 16 carbohydrate binding modules. J Biol Chem 2010, 285:34665-34676.
    • (2010) J Biol Chem , vol.285 , pp. 34665-34676
    • Su, X.1    Agarwal, V.2    Dodd, D.3    Bae, B.4    Mackie, R.I.5    Nair, S.K.6    Cann, I.K.7
  • 45
    • 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
  • 46
    • 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 2003, 11:665-675.
    • (2003) Structure , vol.11 , pp. 665-675
    • Boraston, A.B.1    Revett, T.J.2    Boraston, C.M.3    Nurizzo, D.4    Davies, G.J.5
  • 48
    • 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
  • 49
    • 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
  • 50
    • 0344406252 scopus 로고    scopus 로고
    • The fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activity
    • Leemhuis H., Rozeboom H.J., Dijkstra B.W., Dijkhuizen L. The fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activity. FEBS Lett 2003, 541:47-51.
    • (2003) FEBS Lett , vol.541 , pp. 47-51
    • Leemhuis, H.1    Rozeboom, H.J.2    Dijkstra, B.W.3    Dijkhuizen, L.4
  • 51
    • 56049109995 scopus 로고    scopus 로고
    • Crystal structures of the starch-binding domain from Rhizopus oryzae glucoamylase reveal a polysaccharide-binding path
    • Tung J.Y., Chang M.D., Chou W.I., Liu Y.Y., Yeh Y.H., Chang F.Y., Lin S.C., Qiu Z.L., Sun Y.J. Crystal structures of the starch-binding domain from Rhizopus oryzae glucoamylase reveal a polysaccharide-binding path. Biochem J 2008, 416:27-36.
    • (2008) Biochem J , vol.416 , pp. 27-36
    • Tung, J.Y.1    Chang, M.D.2    Chou, W.I.3    Liu, Y.Y.4    Yeh, Y.H.5    Chang, F.Y.6    Lin, S.C.7    Qiu, Z.L.8    Sun, Y.J.9
  • 52
    • 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., Law V. 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 2006, 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
  • 53
    • 33845683489 scopus 로고    scopus 로고
    • The structural basis of alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima
    • van Bueren A.L., Boraston A.B. The structural basis of alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima. J Mol Biol 2007, 365:555-560.
    • (2007) J Mol Biol , vol.365 , pp. 555-560
    • van Bueren, A.L.1    Boraston, A.B.2
  • 54
    • 75849119359 scopus 로고    scopus 로고
    • SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules
    • Koropatkin N.M., Smith T.J. SusG: a unique cell-membrane-associated alpha-amylase from a prominent human gut symbiont targets complex starch molecules. Structure 2010, 18:200-215.
    • (2010) Structure , vol.18 , pp. 200-215
    • Koropatkin, N.M.1    Smith, T.J.2
  • 55
    • 15244339423 scopus 로고    scopus 로고
    • Crystal structure of maltooligosyltrehalose trehalohydrolase from Deinococcus radiodurans in complex with disaccharides
    • Timmins J., Leiros H.K., Leonard G., Leiros I., McSweeney S. Crystal structure of maltooligosyltrehalose trehalohydrolase from Deinococcus radiodurans in complex with disaccharides. J Mol Biol 2005, 347:949-963.
    • (2005) J Mol Biol , vol.347 , pp. 949-963
    • Timmins, J.1    Leiros, H.K.2    Leonard, G.3    Leiros, I.4    McSweeney, S.5
  • 57
    • 84899464666 scopus 로고    scopus 로고
    • Structural elucidation of the cyclization mechanism of α-1,6-glucan by Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase
    • Epub 2014 Mar 10. PMID: 24616103
    • Suzuki N., Fujimoto Z., Kim Y.M., Momma M., Kishine N., Suzuki R., Suzuki S., Kitamura S., Kobayashi M., Kimura A., et al. Structural elucidation of the cyclization mechanism of α-1,6-glucan by Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase. J Biol Chem. 2014, 289:12040-12051. Epub 2014 Mar 10. PMID: 24616103. 10.1074/jbc.M114.547992.
    • (2014) J Biol Chem. , vol.289 , pp. 12040-12051
    • Suzuki, N.1    Fujimoto, Z.2    Kim, Y.M.3    Momma, M.4    Kishine, N.5    Suzuki, R.6    Suzuki, S.7    Kitamura, S.8    Kobayashi, M.9    Kimura, A.10


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