메뉴 건너뛰기




Volumn 356, Issue 1, 2006, Pages 57-71

Dimerisation and an increase in active site aromatic groups as adaptations to high temperatures: X-ray solution scattering and substrate-bound crystal structures of Rhodothermus marinus endoglucanase Cel12A

Author keywords

Cellulase; Complex structure; Endoglucanase; SAXS; Thermostability

Indexed keywords

CARBOHYDRATE; CELLULASE; GLUCAN SYNTHASE; GLUCOSE; SEA WATER;

EID: 30344484545     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.11.004     Document Type: Article
Times cited : (20)

References (50)
  • 2
    • 0031800087 scopus 로고    scopus 로고
    • Structural studies on cellulases
    • G.J. Davies Structural studies on cellulases Biochem. Soc. Trans. 26 1998 167 173
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 167-173
    • Davies, G.J.1
  • 3
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • A.B. Boraston, D.N. Bolam, H.J. Gilbert, and G.J. Davies Carbohydrate-binding modules: fine-tuning polysaccharide recognition Biochem. J. 382 2004 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
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino-acid sequence similarities
    • B. Henrissat 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
  • 5
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino-acid sequence similarities
    • B. Henrissat, and A. Bairoch 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
  • 6
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • B. Henrissat, and A. Bairoch Updating the sequence-based classification of glycosyl hydrolases Biochem. J. 316 1996 695 696
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 7
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • G. Davies, and B. Henrissat Structures and mechanisms of glycosyl hydrolases Structure 3 1995 853 859
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 8
    • 0000353077 scopus 로고
    • Rhodothermus marinus, gen. nov., sp. nov., a thermophilic, halophilic bacterium from submarine hot springs in Iceland
    • G.A. Alfredsson, J.K. Kristjansson, S. Hjörleifsdottir, and K.O. Stetter Rhodothermus marinus, gen. nov., sp. nov., a thermophilic, halophilic bacterium from submarine hot springs in Iceland J. Gen. Microbiol. 134 1988 299 306
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 299-306
    • Alfredsson, G.A.1    Kristjansson, J.K.2    Hjörleifsdottir, S.3    Stetter, K.O.4
  • 9
    • 0030800010 scopus 로고    scopus 로고
    • Cloning and sequence of a thermostable multidomain xylanase from the bacterium Rhodothermus marinus
    • E. Nordberg-Karlsson, E. Bartonek-Roxå, and O. Holst Cloning and sequence of a thermostable multidomain xylanase from the bacterium Rhodothermus marinus Biochim. Biophys. Acta 1353 1997 118 124
    • (1997) Biochim. Biophys. Acta , vol.1353 , pp. 118-124
    • Nordberg-Karlsson, E.1    Bartonek-Roxå, E.2    Holst, O.3
  • 10
    • 0027933337 scopus 로고
    • Cloning and sequencing of a Rhodothermus marinus gene, bglA, coding for a thermostable β-glucanase and its expression in E. coli
    • R. Spilliaert, G.O. Hreggvidsson, J.K. Kristjansson, G. Eggertsson, and A. Palsdottir Cloning and sequencing of a Rhodothermus marinus gene, bglA, coding for a thermostable β-glucanase and its expression in E. coli Eur. J. Biochem. 224 1994 923 930
    • (1994) Eur. J. Biochem. , vol.224 , pp. 923-930
    • Spilliaert, R.1    Hreggvidsson, G.O.2    Kristjansson, J.K.3    Eggertsson, G.4    Palsdottir, A.5
  • 11
    • 0032190308 scopus 로고    scopus 로고
    • The laminarinase from the thermophilic eubacterium Rhodothermus marinus: Conformation, stability and identification of active site carboxylic acid residues by site-directed mutagenesis
    • M. Krah, R. Misselwitz, O. Politz, K.K. Thomsen, H. Welfle, and R. Borriss The laminarinase from the thermophilic eubacterium Rhodothermus marinus: conformation, stability and identification of active site carboxylic acid residues by site-directed mutagenesis Eur. J. Biochem. 257 1998 101 111
    • (1998) Eur. J. Biochem. , vol.257 , pp. 101-111
    • Krah, M.1    Misselwitz, R.2    Politz, O.3    Thomsen, K.K.4    Welfle, H.5    Borriss, R.6
  • 14
    • 0035010839 scopus 로고    scopus 로고
    • Deletion of a cytotoxic, N-terminal putative signal peptide results in a significant increase in production yields in Escherichia coli and improved specific activity of Cel12A from Rhodothermus marinus
    • K.B. Wicher, M. Abou-Hachem, S. Hallsdórsdottir, S.H. Thorbjarnadóttir, G. Eggertsson, and G.O. Hreggvidsson Deletion of a cytotoxic, N-terminal putative signal peptide results in a significant increase in production yields in Escherichia coli and improved specific activity of Cel12A from Rhodothermus marinus Appl. Microbiol. Biotech. 55 2001 578 584
    • (2001) Appl. Microbiol. Biotech. , vol.55 , pp. 578-584
    • Wicher, K.B.1    Abou-Hachem, M.2    Hallsdórsdottir, S.3    Thorbjarnadó ttir, S.H.4    Eggertsson, G.5    Hreggvidsson, G.O.6
  • 15
    • 0036300754 scopus 로고    scopus 로고
    • The structure of Rhodothermus marinus Cel12A, a highly thermostable family 12 endoglucanase at 1.8 Å resolution
    • S.J. Crennell, G.O. Hreggvidsson, and E. Nordberg-Karlsson The structure of Rhodothermus marinus Cel12A, a highly thermostable family 12 endoglucanase at 1.8 Å resolution J. Mol. Biol. 320 2002 883 897
    • (2002) J. Mol. Biol. , vol.320 , pp. 883-897
    • Crennell, S.J.1    Hreggvidsson, G.O.2    Nordberg-Karlsson, E.3
  • 17
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • A. Szilágyi, and P. Závodszky Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey Structure 8 2000 493 504
    • (2000) Structure , vol.8 , pp. 493-504
    • Szilágyi, A.1    Závodszky, P.2
  • 18
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses and molecular mechanisms for thermostability
    • C. Vieille, and G.J. Zeikus Hyperthermophilic enzymes: sources, uses and molecular mechanisms for thermostability Microbiol. Mol. Biol. Rev. 65 2001 1 43
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 19
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • G.J. Davies, K.S. Wilson, and B. Henrissat Nomenclature for sugar-binding subsites in glycosyl hydrolases Biochem. J. 321 1997 557 559
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 20
    • 0033551103 scopus 로고    scopus 로고
    • The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 Å resolution
    • G. Sulzenbacher, L.F. Mackenzie, K.S. Wilson, S.G. Withers, C. Dupont, and G.J. Davies The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 Å resolution Biochemistry 38 1999 4826 4833
    • (1999) Biochemistry , vol.38 , pp. 4826-4833
    • Sulzenbacher, G.1    MacKenzie, L.F.2    Wilson, K.S.3    Withers, S.G.4    Dupont, C.5    Davies, G.J.6
  • 21
    • 4444264058 scopus 로고    scopus 로고
    • Crystal complex structures reveal how substrate is bound in the -4 to +2 binding sites of Humicola grisea Cel12A
    • M. Sandgren, G.I. Berglund, A. Shaw, J. Ståhlberg, L. Kenne, T. Desmet, and C. Mitchinson Crystal complex structures reveal how substrate is bound in the -4 to +2 binding sites of Humicola grisea Cel12A J. Mol. Biol. 342 2004 1505 1517
    • (2004) J. Mol. Biol. , vol.342 , pp. 1505-1517
    • Sandgren, M.1    Berglund, G.I.2    Shaw, A.3    Ståhlberg, J.4    Kenne, L.5    Desmet, T.6    Mitchinson, C.7
  • 23
    • 12344307441 scopus 로고    scopus 로고
    • Conformational changes observed in enzyme crystal structures upon substrate binding
    • A. Gutteridge, and J. Thornton Conformational changes observed in enzyme crystal structures upon substrate binding J. Mol. Biol. 346 2005 21 28
    • (2005) J. Mol. Biol. , vol.346 , pp. 21-28
    • Gutteridge, A.1    Thornton, J.2
  • 25
    • 0032590072 scopus 로고    scopus 로고
    • An endoglucanase, EglA, from the hyperthermophilic archaeon Pyrococcus furiosus, hydrolyses β-1,4 bonds in mixed-linkage (1→3),(1→4)- β-d-glucans and cellulose
    • M.W. Bauer, L.E. Driskill, W. Callen, M.A. Snead, E.J. Mathur, and R.M. Kelly An endoglucanase, EglA, from the hyperthermophilic archaeon Pyrococcus furiosus, hydrolyses β-1,4 bonds in mixed-linkage (1→3),(1→4)- β-d-glucans and cellulose J. Bacteriol. 181 1999 284 290
    • (1999) J. Bacteriol. , vol.181 , pp. 284-290
    • Bauer, M.W.1    Driskill, L.E.2    Callen, W.3    Snead, M.A.4    Mathur, E.J.5    Kelly, R.M.6
  • 27
    • 0037865396 scopus 로고    scopus 로고
    • Mapping the conformational itinerary of β-glucosidases by X-ray crystallography
    • G.J. Davies, V.M.-A. Ducros, A. Varrot, and D.L. Zechel Mapping the conformational itinerary of β-glucosidases by X-ray crystallography Biochem. Soc. Trans. 31 2003 523 527
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 523-527
    • Davies, G.J.1    Ducros, V.M.-A.2    Varrot, A.3    Zechel, D.L.4
  • 29
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • N. Kannen, and S. Vishveshwara Aromatic clusters: a determinant of thermal stability of thermophilic proteins Protein Eng. 13 2000 753 761
    • (2000) Protein Eng. , vol.13 , pp. 753-761
    • Kannen, N.1    Vishveshwara, S.2
  • 30
    • 0029774346 scopus 로고    scopus 로고
    • Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes
    • W. Liebl, P. Ruile, K. Bronnenmeier, K. Riedel, F. Lottspeich, and I. Greif Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes Microbiology 142 1996 2533 2542
    • (1996) Microbiology , vol.142 , pp. 2533-2542
    • Liebl, W.1    Ruile, P.2    Bronnenmeier, K.3    Riedel, K.4    Lottspeich, F.5    Greif, I.6
  • 31
    • 0032403607 scopus 로고    scopus 로고
    • Purification, characterisation and molecular analysis of thermostable cellulases CelA and CelB from Thermotoga neapolitana
    • J.D. Bok, D.A. Yernool, and D.E. Eveleigh Purification, characterisation and molecular analysis of thermostable cellulases CelA and CelB from Thermotoga neapolitana Appl. Microbiol. Biotechnol. 64 1998 4774 4781
    • (1998) Appl. Microbiol. Biotechnol. , vol.64 , pp. 4774-4781
    • Bok, J.D.1    Yernool, D.A.2    Eveleigh, D.E.3
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • (Carter, C. W., Jr & Sweet, R. M., eds), Academic Press, New York.
    • Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology (Carter, C. W., Jr & Sweet, R. M., eds), vol. 276, pp. 307-326, Academic Press, New York.
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 84889120137 scopus 로고
    • Improved methods for building models in electron-density maps and the location of errors in these models
    • T.A. Jones, J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building 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
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system (CNS): A new software system for macromolecular structure determination
    • A.T. Brunger, P.D. Adams, G.M. Clore, W.L. DeLano, and P. Gros Crystallography and NMR system (CNS): a new software system for macromolecular structure determination Acta Crystallog. sect. D 54 1998 905 921
    • (1998) Acta Crystallog. Sect. D , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, G.M.3    Delano, W.L.4    Gros, P.5
  • 35
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • G.J. Kleywegt 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
    • 0030831667 scopus 로고    scopus 로고
    • α coordinates alone
    • α coordinates alone J. Mol. Biol. 273 1997 371 376
    • (1997) J. Mol. Biol. , vol.273 , pp. 371-376
    • Kleywegt, G.J.1
  • 37
    • 0020114103 scopus 로고
    • X-ray diffraction and scattering on disordered systems using synchrotron radiation
    • M.H.J. Koch, and J. Bordas X-ray diffraction and scattering on disordered systems using synchrotron radiation Nucl. Instrum. Methods 208 1983 461 469
    • (1983) Nucl. Instrum. Methods , vol.208 , pp. 461-469
    • Koch, M.H.J.1    Bordas, J.2
  • 38
    • 0024033744 scopus 로고
    • Data acquisition systems for linear and area X-ray detectors using delay line readout
    • C.J. Boulin, R. Kempf, A. Gabriel, and M.H.J. Koch Data acquisition systems for linear and area X-ray detectors using delay line readout Nucl. Instrum. Methods A 269 1988 312 320
    • (1988) Nucl. Instrum. Methods a , vol.269 , pp. 312-320
    • Boulin, C.J.1    Kempf, R.2    Gabriel, A.3    Koch, M.H.J.4
  • 39
  • 42
    • 0027578071 scopus 로고
    • A direct indirect method of small-angle scattering data treatment
    • D.I. Svergun A direct indirect method of small-angle scattering data treatment J. Appl. Crystallog. 26 1993 258 267
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 258-267
    • Svergun, D.I.1
  • 43
    • 0001498978 scopus 로고
    • La diffraction des rayons X aux tres petits angles; Application a l'etude de phenomenes ultramicroscopiques
    • A. Guinier La diffraction des rayons X aux tres petits angles; application a l'etude de phenomenes ultramicroscopiques Ann. Phys. (Paris) 12 1939 161 237
    • (1939) Ann. Phys. (Paris) , vol.12 , pp. 161-237
    • Guinier, A.1
  • 44
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularization parameter in indirect transform methods using perceptual criteria J. Appl. Crystallog. 495 1992 503
    • (1992) J. Appl. Crystallog. , vol.495 , pp. 503
    • Svergun, D.I.1
  • 45
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • D.I. Svergun, C. Barberato, and M.H.J. Koch CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallog. 28 1995 768 773
    • (1995) J. Appl. Crystallog. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 46
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • M.V. Petoukhov, and D.I. Svergun Global rigid body modeling of macromolecular complexes against small-angle scattering data Biophys. J. 89 2005 1237 1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 47
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 48
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 49
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MOLSCRIPT that includes greatly enhanced colouring capacities
    • R.E. Esnouf An extensively modified version of MOLSCRIPT that includes greatly enhanced colouring capacities J. Mol. Graph. Modelling 15 1997 132 136
    • (1997) J. Mol. Graph. Modelling , vol.15 , pp. 132-136
    • Esnouf, R.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.