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Volumn 288, Issue 11, 2013, Pages 7978-7985

Small angle x-ray scattering analysis of clostridium thermocellum cellulosome N-terminal complexes reveals a highly dynamic structure

Author keywords

[No Author keywords available]

Indexed keywords

CLOSTRIDIUM; DISTRIBUTION FUNCTIONS; ENZYMES;

EID: 84875189918     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.408757     Document Type: Article
Times cited : (22)

References (41)
  • 2
    • 67650215053 scopus 로고    scopus 로고
    • Lignocellulose conversion to biofuels: Current challenges, global perspectives
    • Himmel, M. E., and Bayer, E. A. (2009) Lignocellulose conversion to biofuels: current challenges, global perspectives. Curr. Opin. Biotechnol. 20, 316-317
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 316-317
    • Himmel, M.E.1    Bayer, E.A.2
  • 4
    • 0029843079 scopus 로고    scopus 로고
    • Microbial hydrolysis of polysaccharides
    • Warren, R. A. (1996) Microbial hydrolysis of polysaccharides. Annu. Rev. Microbiol. 50, 183-212
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 183-212
    • Warren, R.A.1
  • 5
    • 4143139469 scopus 로고    scopus 로고
    • The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides
    • Bayer, E. A., Belaich, J. P., Shoham, Y., and Lamed, R. (2004) The cellulosomes: multienzyme machines for degradation of plant cell wall polysaccharides. Annu. Rev. Microbiol. 58, 521-554
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 521-554
    • Bayer, E.A.1    Belaich, J.P.2    Shoham, Y.3    Lamed, R.4
  • 7
    • 3142757398 scopus 로고    scopus 로고
    • Cellulosomes: Plant-cell-wall-degrading enzyme complexes
    • Doi, R. H., and Kosugi, A. (2004) Cellulosomes: plant-cell-wall-degrading enzyme complexes. Nat. Rev. Microbiol. 2, 541-551
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 541-551
    • Doi, R.H.1    Kosugi, A.2
  • 8
    • 77953631886 scopus 로고    scopus 로고
    • Cellulosomes: Highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates
    • Fontes, C. M., and Gilbert, H. J. (2010) Cellulosomes: highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates. Annu. Rev. Biochem. 79, 655-681
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 655-681
    • Fontes, C.M.1    Gilbert, H.J.2
  • 9
    • 33947256880 scopus 로고    scopus 로고
    • Cellulosomes: Microbial nanomachines that display plasticity in quaternary structure
    • Gilbert, H. J. (2007) Cellulosomes: microbial nanomachines that display plasticity in quaternary structure. Mol. Microbiol. 63, 1568-1576
    • (2007) Mol. Microbiol. , vol.63 , pp. 1568-1576
    • Gilbert, H.J.1
  • 10
    • 0027984011 scopus 로고
    • The cellulosome-a treasuretrove for biotechnology
    • Bayer, E. A., Morag, E., and Lamed, R. (1994) The cellulosome-a treasuretrove for biotechnology. Trends Biotechnol. 12, 379-386
    • (1994) Trends Biotechnol , vol.12 , pp. 379-386
    • Bayer, E.A.1    Morag, E.2    Lamed, R.3
  • 11
    • 0031799314 scopus 로고    scopus 로고
    • The cellulosome of Clostridium thermocellum
    • Béguin, P., and Alzari, P. M. (1998) The cellulosome of Clostridium thermocellum. Biochem. Soc. Trans. 26, 178-185
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 178-185
    • Béguin, P.1    Alzari, P.M.2
  • 12
    • 0020958567 scopus 로고
    • The cellulosome: A discrete cell surface organelle of Clostridium thermocellum which exhibits separate antigenic, cellulose-binding and various cellulolytic activities
    • Lamed, R., Setter, E., Kenig, R., and Bayer, E. A. (1983) The cellulosome: a discrete cell surface organelle of Clostridium thermocellum which exhibits separate antigenic, cellulose-binding and various cellulolytic activities. Biotechnol. Bioeng. Symp. 13, 163-181
    • (1983) Biotechnol. Bioeng. Symp. , vol.13 , pp. 163-181
    • Lamed, R.1    Setter, E.2    Kenig, R.3    Bayer, E.A.4
  • 13
    • 0021016163 scopus 로고
    • Characterization of a cellulose-binding, cellulase-containing complex in Clostridium thermocellum
    • Lamed, R., Setter, E., and Bayer, E. A. (1983) Characterization of a cellulose-binding, cellulase-containing complex in Clostridium thermocellum. J. Bacteriol. 156, 828-836
    • (1983) J. Bacteriol. , vol.156 , pp. 828-836
    • Lamed, R.1    Setter, E.2    Bayer, E.A.3
  • 16
    • 0027285934 scopus 로고
    • Sequencing of a Clostridium thermocellum gene (cipA) encoding the cellulosomal SL-protein reveals an unusual degree of internal homology
    • Gerngross, U. T., Romaniec, M. P., Kobayashi, T., Huskisson, N. S., and Demain, A. L. (1993) Sequencing of a Clostridium thermocellum gene (cipA) encoding the cellulosomal SL-protein reveals an unusual degree of internal homology. Mol. Microbiol. 8, 325-334
    • (1993) Mol. Microbiol. , vol.8 , pp. 325-334
    • Gerngross, U.T.1    Romaniec, M.P.2    Kobayashi, T.3    Huskisson, N.S.4    Demain, A.L.5
  • 17
    • 0026621578 scopus 로고
    • Identification of the cellulose-binding domain of the cellulosome subunit S1 from Clostridium thermocellum YS
    • Poole, D. M., Morag, E., Lamed, R., Bayer, E. A., Hazlewood, G. P., and Gilbert, H. J. (1992) Identification of the cellulose-binding domain of the cellulosome subunit S1 from Clostridium thermocellum YS. FEMS Microbiol. Lett. 78, 181-186
    • (1992) FEMS Microbiol. Lett. , vol.78 , pp. 181-186
    • Poole, D.M.1    Morag, E.2    Lamed, R.3    Bayer, E.A.4    Hazlewood, G.P.5    Gilbert, H.J.6
  • 18
    • 0037133136 scopus 로고    scopus 로고
    • Duplicated dockerin subdomains of Clostridium thermocellum endoglucanase CelD bind to a cohesin domain of the scaffolding protein CipA with distinct thermodynamic parameters and a negative cooperativity
    • Schaeffer, F., Matuschek, M., Guglielmi, G., Miras, I., Alzari, P. M., and Béguin, P. (2002) Duplicated dockerin subdomains of Clostridium thermocellum endoglucanase CelD bind to a cohesin domain of the scaffolding protein CipA with distinct thermodynamic parameters and a negative cooperativity. Biochemistry 41, 2106-2114
    • (2002) Biochemistry , vol.41 , pp. 2106-2114
    • Schaeffer, F.1    Matuschek, M.2    Guglielmi, G.3    Miras, I.4    Alzari, P.M.5    Béguin, P.6
  • 19
    • 0029955959 scopus 로고    scopus 로고
    • Crystal structure of a bacterial family-III cellulosebinding 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 cellulosebinding 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
  • 20
    • 43049170350 scopus 로고    scopus 로고
    • Crystal structure of a cellulosomal family 3 carbohydrate esterase from Clostridium thermocellum provides insights into the mechanism of substrate recognition
    • Correia, M. A., Prates, J. A., Brás, J., Fontes, C. M., Newman, J. A., Lewis, R. J., Gilbert, H. J., and Flint, J. E. (2008) Crystal structure of a cellulosomal family 3 carbohydrate esterase from Clostridium thermocellum provides insights into the mechanism of substrate recognition. J. Mol. Biol. 379, 64-72
    • (2008) J. Mol. Biol. , vol.379 , pp. 64-72
    • Correia, M.A.1    Prates, J.A.2    Brás, J.3    Fontes, C.M.4    Newman, J.A.5    Lewis, R.J.6    Gilbert, H.J.7    Flint, J.E.8
  • 21
    • 0036310985 scopus 로고    scopus 로고
    • The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum cellulosome
    • Guimarães, B. G., Souchon, H., Lytle, B. L., Wu, J. H. D., and Alzari, P. M. (2002) The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum cellulosome. J. Mol. Biol. 320, 587-596
    • (2002) J. Mol. Biol. , vol.320 , pp. 587-596
    • Guimarães, B.G.1    Souchon, H.2    Lytle, B.L.3    Wu, J.H.D.4    Alzari, P.M.5
  • 22
    • 37249000280 scopus 로고    scopus 로고
    • Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum
    • Kitago, Y., Karita, S., Watanabe, N., Kamiya, M., Aizawa, T., Sakka, K., and Tanaka, I. (2007) Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J. Biol. Chem. 282, 35703-35711
    • (2007) J. Biol. Chem. , vol.282 , pp. 35703-35711
    • Kitago, Y.1    Karita, S.2    Watanabe, N.3    Kamiya, M.4    Aizawa, T.5    Sakka, K.6    Tanaka, I.7
  • 23
    • 0035970297 scopus 로고    scopus 로고
    • Solution structure of a type i dockerin domain, a novel prokaryotic, extracellular calcium-binding domain
    • Lytle, B. L., Volkman, B. F., Westler, W. M., Heckman, M. P., and Wu, J. H. (2001) Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain. J. Mol. Biol. 307, 745-753
    • (2001) J. Mol. Biol. , vol.307 , pp. 745-753
    • Lytle, B.L.1    Volkman, B.F.2    Westler, W.M.3    Heckman, M.P.4    Wu, J.H.5
  • 24
    • 0031569395 scopus 로고    scopus 로고
    • A cohesin domain from Clostridium thermocellum: The crystal structure provides new insights into cellulosome assembly
    • Shimon, L. J., Bayer, E. A., Morag, E., Lamed, R., Yaron, S., Shoham, Y., and Frolow, F. (1997) A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly. Structure 5, 381-390
    • (1997) Structure , vol.5 , pp. 381-390
    • Shimon, L.J.1    Bayer, E.A.2    Morag, E.3    Lamed, R.4    Yaron, S.5    Shoham, Y.6    Frolow, F.7
  • 25
    • 0031592929 scopus 로고    scopus 로고
    • The crystal structure of a type i cohesin domain at 1.7 Å resolution
    • Tavares, G. A., Béguin, P., and Alzari, P. M. (1997) The crystal structure of a type I cohesin domain at 1.7 Å resolution. J. Mol. Biol. 273, 701-713
    • (1997) J. Mol. Biol. , vol.273 , pp. 701-713
    • Tavares, G.A.1    Béguin, P.2    Alzari, P.M.3
  • 26
    • 78650417465 scopus 로고    scopus 로고
    • Synergy, structure and conformational flexibility of hybrid cellulosomes displaying various inter-cohesin linkers
    • Molinier, A. L., Nouailler, M., Valette, O., Tardif, C., Receveur-Bréchot, V., and Fierobe, H. P. (2011) Synergy, structure and conformational flexibility of hybrid cellulosomes displaying various inter-cohesin linkers. J. Mol. Biol. 405, 143-157
    • (2011) J. Mol. Biol. , vol.405 , pp. 143-157
    • Molinier, A.L.1    Nouailler, M.2    Valette, O.3    Tardif, C.4    Receveur-Bréchot, V.5    Fierobe, H.P.6
  • 27
    • 0022512490 scopus 로고
    • Ultrastructure of the cell surface cellulosome of Clostridium thermocellum and its interaction with cellulose
    • Bayer, E. A., and Lamed, R. (1986) Ultrastructure of the cell surface cellulosome of Clostridium thermocellum and its interaction with cellulose. J. Bacteriol. 167, 828-836
    • (1986) J. Bacteriol. , vol.167 , pp. 828-836
    • Bayer, E.A.1    Lamed, R.2
  • 28
    • 0001728210 scopus 로고
    • Macromolecular organization of the cellulolytic enzyme complex of Clostridium thermocellum as revealed by electron microscopy
    • Mayer, F., Coughlan, M. P., Mori, Y., and Ljungdahl, L. G. (1987) Macromolecular organization of the cellulolytic enzyme complex of Clostridium thermocellum as revealed by electron microscopy. Appl. Environ. Microbiol. 53, 2785-2792
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 2785-2792
    • Mayer, F.1    Coughlan, M.P.2    Mori, Y.3    Ljungdahl, L.G.4
  • 31
    • 75649147383 scopus 로고    scopus 로고
    • The molecular weight of proteins in solution can be determined from a single SAXS measurement on a relative scale
    • Fischer, H., de Oliveira Neto, M., Napolitano, H. B., Polikarpov, I., and Craievich, A. F. (2010) The molecular weight of proteins in solution can be determined from a single SAXS measurement on a relative scale. J. Appl. Crystallogr. 43, 101-109
    • (2010) J. Appl. Crystallogr. , vol.43 , pp. 101-109
    • Fischer, H.1    De Oliveira Neto, M.2    Napolitano, H.B.3    Polikarpov, I.4    Craievich, A.F.5
  • 32
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76, 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 33
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from x-ray solution scattering
    • Svergun, D. I., Petoukhov, M. V., and Koch, M. H. (2001) Determination of domain structure of proteins from x-ray solution scattering. Biophys. J. 80, 2946-2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 34
    • 67650992092 scopus 로고    scopus 로고
    • Structure and flexibility within proteins as identified through small angle X-ray scattering
    • Pelikan, M., Hura, G. L., and Hammel, M. (2009) Structure and flexibility within proteins as identified through small angle X-ray scattering. Gen. Physiol. Biophys. 28, 174-189
    • (2009) Gen. Physiol. Biophys. , vol.28 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 35
    • 0030584665 scopus 로고    scopus 로고
    • The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum
    • Alzari, P. M., Souchon, H., and Dominguez, R. (1996) The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum. Structure 4, 265-275
    • (1996) Structure , vol.4 , pp. 265-275
    • Alzari, P.M.1    Souchon, H.2    Dominguez, R.3
  • 37
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley, L. A., and Sternberg, M. J. (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4, 363-371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 38
    • 11244296147 scopus 로고    scopus 로고
    • Structural insights into the mechanism of formation of cellulosomes probed by small angle x-ray scattering
    • Hammel, M., Fierobe, H. P., Czjzek, M., Finet, S., and Receveur-Bréchot, V. (2004) Structural insights into the mechanism of formation of cellulosomes probed by small angle x-ray scattering. J. Biol. Chem. 279, 55985-55994
    • (2004) J. Biol. Chem. , vol.279 , pp. 55985-55994
    • Hammel, M.1    Fierobe, H.P.2    Czjzek, M.3    Finet, S.4    Receveur-Bréchot, V.5
  • 40
    • 77649274709 scopus 로고    scopus 로고
    • Insights into higher-order organization of the cellulosome revealed by a dissect-and-build approach: Crystal structure of interacting Clostridium thermocellum multimodular components
    • Adams, J. J., Currie, M. A., Ali, S., Bayer, E. A., Jia, Z., and Smith, S. P. (2010) Insights into higher-order organization of the cellulosome revealed by a dissect-and-build approach: crystal structure of interacting Clostridium thermocellum multimodular components. J. Mol. Biol. 396, 833-839
    • (2010) J. Mol. Biol. , vol.396 , pp. 833-839
    • Adams, J.J.1    Currie, M.A.2    Ali, S.3    Bayer, E.A.4    Jia, Z.5    Smith, S.P.6
  • 41
    • 84864555920 scopus 로고    scopus 로고
    • Scaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosome
    • Currie, M. A., Adams, J. J., Faucher, F., Bayer, E. A., Jia, Z., and Smith, S. P. (2012) Scaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosome. J. Biol. Chem. 287, 26953-26961
    • (2012) J. Biol. Chem. , vol.287 , pp. 26953-26961
    • Currie, M.A.1    Adams, J.J.2    Faucher, F.3    Bayer, E.A.4    Jia, Z.5    Smith, S.P.6


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