메뉴 건너뛰기




Volumn 79, Issue 1, 2011, Pages 50-60

Noncellulosomal cohesin from the hyperthermophilic archaeon Archaeoglobus fulgidus

Author keywords

Dockerin; Protein oligomerization; Thermostability; X ray crystallography

Indexed keywords

CELLULOSOME; COHESIN; DIMER; TETRAMER;

EID: 78649770974     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22857     Document Type: Article
Times cited : (6)

References (50)
  • 1
    • 0021016163 scopus 로고
    • Characterization of a cellulose-binding, cellulase-containing complex in Clostridium thermocellum
    • Lamed R, Setter E, Bayer EA. Characterization of a cellulose-binding, cellulase-containing complex in Clostridium thermocellum. J Bacteriol 1983; 156: 828-836.
    • (1983) J Bacteriol , vol.156 , pp. 828-836
    • Lamed, R.1    Setter, E.2    Bayer, E.A.3
  • 2
    • 0033405884 scopus 로고    scopus 로고
    • Cellulosome-like sequences in Archaeoglobus fulgidus: an enigmatic vestige of cohesin and dockerin domains
    • Bayer EA, Coutinho PM, Henrissat B. Cellulosome-like sequences in Archaeoglobus fulgidus: an enigmatic vestige of cohesin and dockerin domains. FEBS Lett 1999; 463: 277-280.
    • (1999) FEBS Lett , vol.463 , pp. 277-280
    • Bayer, E.A.1    Coutinho, P.M.2    Henrissat, B.3
  • 5
    • 36348998694 scopus 로고    scopus 로고
    • Three-dimensional structure of a putative non-cellulosomal cohesin module from a Clostridium perfringens family 84 glycoside hydrolase
    • Chitayat S, Gregg K, Adams JJ, Ficko-Blean E, Bayer EA, Boraston AB, Smith SP. Three-dimensional structure of a putative non-cellulosomal cohesin module from a Clostridium perfringens family 84 glycoside hydrolase. J Mol Biol 2008; 375: 20-28.
    • (2008) J Mol Biol , vol.375 , pp. 20-28
    • Chitayat, S.1    Gregg, K.2    Adams, J.J.3    Ficko-Blean, E.4    Bayer, E.A.5    Boraston, A.B.6    Smith, S.P.7
  • 8
    • 27744458385 scopus 로고    scopus 로고
    • Matching fusion protein systems for affinity analysis of two interacting families of proteins: the cohesin-dockerin interaction
    • Barak Y, Handelsman T, Nakar D, Mechaly A, Lamed R, Shoham Y, Bayer EA. Matching fusion protein systems for affinity analysis of two interacting families of proteins: the cohesin-dockerin interaction. J Mol Recognit 2005; 18: 491-501.
    • (2005) J Mol Recognit , vol.18 , pp. 491-501
    • Barak, Y.1    Handelsman, T.2    Nakar, D.3    Mechaly, A.4    Lamed, R.5    Shoham, Y.6    Bayer, E.A.7
  • 9
    • 0038443570 scopus 로고    scopus 로고
    • The cellulosome system of Acetivibrio cellulolyticus includes a novel type of adaptor protein and a cell surface anchoring protein
    • Xu Q, Gao W, Ding SY, Kenig R, Shoham Y, Bayer EA, Lamed R. The cellulosome system of Acetivibrio cellulolyticus includes a novel type of adaptor protein and a cell surface anchoring protein. J Bacteriol 2003; 185: 4548-4557.
    • (2003) J Bacteriol , vol.185 , pp. 4548-4557
    • Xu, Q.1    Gao, W.2    Ding, S.Y.3    Kenig, R.4    Shoham, Y.5    Bayer, E.A.6    Lamed, R.7
  • 14
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 2001; 305: 567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 17
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M, Kumar S. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 2007; 24: 1596-1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 18
    • 0003902144 scopus 로고
    • X-ray structure determination. A practical guide
    • London, Macmillan;
    • Stout GH, Jensen LH. X-ray structure determination. A practical guide. London: Macmillan; 1968.
    • (1968)
    • Stout, G.H.1    Jensen, L.H.2
  • 19
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read RJ. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr Sect D Biol Crystallogr 2001; 57: 1373-1382.
    • (2001) Acta Crystallogr Sect D Biol Crystallogr , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 20
    • 0028103275 scopus 로고
    • The CCP4 Suite-programs for protein crystallography
    • Bailey S. The CCP4 Suite-programs for protein crystallography. Acta Cryst D 1994; 50: 760-763.
    • (1994) Acta Cryst D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 23
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, Lamzin VS. Automated protein model building combined with iterative structure refinement. Nature Struct Biol 1999; 6: 458-463.
    • (1999) Nature Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 26
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Cryst A 1991; 47: 110-119.
    • (1991) Acta Cryst A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0026597444 scopus 로고
    • Free R-value-a novel statistical quantity for assessing the accuracy of crystal-structures
    • Brunger AT. Free R-value-a novel statistical quantity for assessing the accuracy of crystal-structures. Nature 1992; 355: 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 30
    • 0033613813 scopus 로고    scopus 로고
    • Recognition of spatial motifs in protein structures
    • Kleywegt GJ. Recognition of spatial motifs in protein structures. J Mol Biol 1999; 285: 1887-1897.
    • (1999) J Mol Biol , vol.285 , pp. 1887-1897
    • Kleywegt, G.J.1
  • 32
    • 3242886389 scopus 로고    scopus 로고
    • MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis IW, Murray LW, Richardson JS, Richardson DC. MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res 2004; 32(Web Server issue): W615-W619.
    • (2004) Nucleic Acids Res , vol.32
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 33
    • 0003845223 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system
    • San Carlos, CA, DeLano Scientific LLC;
    • DeLano WL. The PyMOL molecular graphics system. San Carlos, CA: DeLano Scientific LLC; 2002.
    • (2002)
    • DeLano, W.L.1
  • 34
    • 58149277107 scopus 로고    scopus 로고
    • Noncellulosomal cohesin- and dockerin-like modules in the three domains of life
    • Peer A, Smith SP, Bayer EA, Lamed R, Borovok I. Noncellulosomal cohesin- and dockerin-like modules in the three domains of life. FEMS Microbiol Lett 2009; 291: 1-16.
    • (2009) FEMS Microbiol Lett , vol.291 , pp. 1-16
    • Peer, A.1    Smith, S.P.2    Bayer, E.A.3    Lamed, R.4    Borovok, I.5
  • 35
    • 0034661436 scopus 로고    scopus 로고
    • Secondary structure and calcium-induced folding of the Clostridium thermocellum dockerin domain determined by NMR spectroscopy
    • Lytle B, Volkman BF, Westler WM, Wu JHD. Secondary structure and calcium-induced folding of the Clostridium thermocellum dockerin domain determined by NMR spectroscopy. Arch Biochem Biophys 2000; 379: 237-244.
    • (2000) Arch Biochem Biophys , vol.379 , pp. 237-244
    • Lytle, B.1    Volkman, B.F.2    Westler, W.M.3    Wu, J.H.D.4
  • 36
    • 0343229549 scopus 로고    scopus 로고
    • Species-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: prediction of specificity determinants of the dockerin domain
    • Pagès S, Belaich A, Belaich J-P, Morag E, Lamed R, Shoham Y, Bayer EA. Species-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: prediction of specificity determinants of the dockerin domain. Proteins 1997; 29: 517-527.
    • (1997) Proteins , vol.29 , pp. 517-527
    • Pagès, S.1    Belaich, A.2    Belaich, J.3    Morag, E.4    Lamed, R.5    Shoham, Y.6    Bayer, E.A.7
  • 37
    • 41149118473 scopus 로고    scopus 로고
    • Cohesin-dockerin microarray: diverse specificities between two complementary families of interacting protein modules
    • Haimovitz R, Barak Y, Morag E, Voronov-Goldman M, Shoham Y, Lamed R, Bayer EA. Cohesin-dockerin microarray: diverse specificities between two complementary families of interacting protein modules. Proteomics 2008; 8: 968-979.
    • (2008) Proteomics , vol.8 , pp. 968-979
    • Haimovitz, R.1    Barak, Y.2    Morag, E.3    Voronov-Goldman, M.4    Shoham, Y.5    Lamed, R.6    Bayer, E.A.7
  • 38
    • 0141939503 scopus 로고    scopus 로고
    • Fitting models to biological data using linear and nonlinear regression. A practical guide to curve fitting
    • San Diego, CA, GraphPad Software Inc.;
    • Motulsky HJ, Christopoulos A. Fitting models to biological data using linear and nonlinear regression. A practical guide to curve fitting. San Diego, CA: GraphPad Software Inc.; 2003. 351 p.
    • (2003) , pp. 351
    • Motulsky, H.J.1    Christopoulos, A.2
  • 39
    • 0034711422 scopus 로고    scopus 로고
    • Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition
    • Spinelli S, Fierobe HP, Belaich A, Belaich JP, Henrissat B, Cambillau C. Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition. J Mol Biol 2000; 304: 189-200.
    • (2000) J Mol Biol , vol.304 , pp. 189-200
    • Spinelli, S.1    Fierobe, H.P.2    Belaich, A.3    Belaich, J.P.4    Henrissat, B.5    Cambillau, C.6
  • 40
    • 16244409867 scopus 로고    scopus 로고
    • Crystal structure of a type-II cohesin module from the Bacteroides cellulosolvens cellulosome reveals novel and distinctive secondary structural elements
    • Noach I, Frolow F, Jakoby H, Rosenheck S, Shimon LW, Lamed R, Bayer EA. Crystal structure of a type-II cohesin module from the Bacteroides cellulosolvens cellulosome reveals novel and distinctive secondary structural elements. J Mol Biol 2005; 348: 1-12.
    • (2005) J Mol Biol , vol.348 , pp. 1-12
    • Noach, I.1    Frolow, F.2    Jakoby, H.3    Rosenheck, S.4    Shimon, L.W.5    Lamed, R.6    Bayer, E.A.7
  • 41
    • 0031569395 scopus 로고    scopus 로고
    • A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly
    • Shimon LJ, Bayer EA, Morag E, Lamed R, Yaron S, Shoham Y, Frolow F. A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly. Structure 1997; 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
  • 42
    • 0032128419 scopus 로고    scopus 로고
    • Miscellaneous algorithms for density modification
    • Cowtan K, Main P. Miscellaneous algorithms for density modification. Acta Cryst D 1998; 54: 487-493.
    • (1998) Acta Cryst D , vol.54 , pp. 487-493
    • Cowtan, K.1    Main, P.2
  • 43
    • 67651115623 scopus 로고    scopus 로고
    • Inter-modular linker flexibility revealed from crystal structures of adjacent cellulosomal cohesins of Acetivibrio cellulolyticus
    • Noach I, Frolow F, Alber O, Lamed R, Shimon LJW, Bayer EA. Inter-modular linker flexibility revealed from crystal structures of adjacent cellulosomal cohesins of Acetivibrio cellulolyticus. J Mol Biol 2009; 391: 86-97.
    • (2009) J Mol Biol , vol.391 , pp. 86-97
    • Noach, I.1    Frolow, F.2    Alber, O.3    Lamed, R.4    Shimon, L.J.W.5    Bayer, E.A.6
  • 44
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L, Park J. DaliLite workbench for protein structure comparison. Bioinformatics 2000; 16: 566-567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 45
    • 0031592929 scopus 로고    scopus 로고
    • The crystal structure of a type I cohesin domain at 1.7 Å resolution
    • Tavares GA, Beguin P, Alzari PM. The crystal structure of a type I cohesin domain at 1.7 Å resolution. J Mol Biol 1997; 273: 701-713.
    • (1997) J Mol Biol , vol.273 , pp. 701-713
    • Tavares, G.A.1    Beguin, P.2    Alzari, P.M.3
  • 47
    • 31044452624 scopus 로고    scopus 로고
    • Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex
    • Adams JJ, Pal G, Jia Z, Smith SP. Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex. Proc Natl Acad Sci USA 2006; 103: 305-310.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 305-310
    • Adams, J.J.1    Pal, G.2    Jia, Z.3    Smith, S.P.4
  • 48
    • 33846650968 scopus 로고    scopus 로고
    • The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli
    • Gerding MA, Ogata Y, Pecora ND, Niki H, de Boer PA. The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Mol Microbiol 2007; 63: 1008-1025.
    • (2007) Mol Microbiol , vol.63 , pp. 1008-1025
    • Gerding, M.A.1    Ogata, Y.2    Pecora, N.D.3    Niki, H.4    de Boer, P.A.5
  • 49
    • 0036093944 scopus 로고    scopus 로고
    • The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB
    • Walburger A, Lazdunski C, Corda Y. The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB. Mol Microbiol 2002; 44: 695-708.
    • (2002) Mol Microbiol , vol.44 , pp. 695-708
    • Walburger, A.1    Lazdunski, C.2    Corda, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.