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Volumn 5, Issue 6, 2010, Pages

The critical role of N- and C-terminal contact in protein stability and folding of a family 10 xylanase under extreme conditions

Author keywords

[No Author keywords available]

Indexed keywords

DODECYL SULFATE SODIUM; MUTANT PROTEIN; PROTEINASE K; TRYPSIN; XYLAN ENDO 1,3 BETA XYLOSIDASE; CARBON; NITROGEN; XYLAN 1,4 BETA XYLOSIDASE;

EID: 77956204645     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0011347     Document Type: Article
Times cited : (40)

References (50)
  • 1
    • 0024529940 scopus 로고
    • Structural principles of alpha/beta barrel proteins: The interior of the sheet
    • Lesk AM, Brändén CI, Chothia C (1989) Structural principles of alpha/beta barrel proteins: the interior of the sheet. Proteins 5: 139-148.
    • (1989) Proteins , vol.5 , pp. 139-148
    • Lesk, A.M.1    Brändén, C.I.2    Chothia, C.3
  • 2
    • 0025876842 scopus 로고
    • Energetic approach to the folding of alpha/beta barrels
    • Chou KC, Carlacci L (1991) Energetic approach to the folding of alpha/beta barrels. Proteins 9: 280-295.
    • (1991) Proteins , vol.9 , pp. 280-295
    • Chou, K.C.1    Carlacci, L.2
  • 3
    • 7344268579 scopus 로고    scopus 로고
    • An analysis of the amino acid clustering pattern in (alpha/beta)8 barrel proteins
    • Selvaraj S, Gromiha MM (1998) An analysis of the amino acid clustering pattern in (alpha/beta)8 barrel proteins. J Protein Chem 17: 407-415.
    • (1998) J Protein Chem , vol.17 , pp. 407-415
    • Selvaraj, S.1    Gromiha, M.M.2
  • 4
    • 0030921675 scopus 로고    scopus 로고
    • Structural basis of the properties of an industrially relevant thermophilic xylanase
    • Harris GW, Pickersgill RW, Connerton I, Debeire P, Touzel JP, et al. (1997) Structural basis of the properties of an industrially relevant thermophilic xylanase. Proteins 29: 77-86.
    • (1997) Proteins , vol.29 , pp. 77-86
    • Harris, G.W.1    Pickersgill, R.W.2    Connerton, I.3    Debeire, P.4    Touzel, J.P.5
  • 5
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • Kannan N, Vishveshwara S (2000) Aromatic clusters: a determinant of thermal stability of thermophilic proteins. Protein Eng 13: 753-761.
    • (2000) Protein Eng , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 6
    • 0034041260 scopus 로고    scopus 로고
    • Cloning, expression, and sequence analysis of the gene encoding the alkali-stable, thermostable endoxylanase from alkalophilic, mesophilic Bacillus Sp. strain NG-27
    • Gupta N, Reddy VS, Maiti S, Ghosh A (2000) Cloning, expression, and sequence analysis of the gene encoding the alkali-stable, thermostable endoxylanase from alkalophilic, mesophilic Bacillus Sp. strain NG-27. Appl Environ Microbiol 66: 2631-2635.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2631-2635
    • Gupta, N.1    Reddy, V.S.2    Maiti, S.3    Ghosh, A.4
  • 8
    • 33746528621 scopus 로고    scopus 로고
    • Crystal structures of native and xylosaccharide-bound alkali thermostable xylanase from an alkalophilic Bacillus sp. NG-27: Structural insights into alkalophilicity and implications for adaptation to polyextreme conditions
    • Manikandan K, Bhardwaj A, Gupta N, Lokanath NK, Ghosh A, et al. (2006) Crystal structures of native and xylosaccharide-bound alkali thermostable xylanase from an alkalophilic Bacillus sp. NG-27: Structural insights into alkalophilicity and implications for adaptation to polyextreme conditions. Protein Sci 15: 1951-1960.
    • (2006) Protein Sci , vol.15 , pp. 1951-1960
    • Manikandan, K.1    Bhardwaj, A.2    Gupta, N.3    Lokanath, N.K.4    Ghosh, A.5
  • 9
    • 51849137782 scopus 로고    scopus 로고
    • The critical role of partially exposed N-terminal valine residue in stabilizing GH10 xylanase from Bacillus sp. NG-27 under poly-extreme conditions
    • doi:10.1371/journal.pone.0003063
    • Bharadwaj A, Leelavathi S, Mazumdar-Leighton S, Ghosh A, Ramakumar S, et al. (2008) The critical role of partially exposed N-terminal valine residue in stabilizing GH10 xylanase from Bacillus sp. NG-27 under poly-extreme conditions. PLoS ONE 3(8): doi:10.1371/journal.pone.0003063.
    • (2008) PLoS ONE , vol.3 , Issue.8
    • Bharadwaj, A.1    Leelavathi, S.2    Mazumdar-Leighton, S.3    Ghosh, A.4    Ramakumar, S.5
  • 10
    • 0037620640 scopus 로고    scopus 로고
    • SCide: Identification of stabilization centers in proteins
    • Dosztányi Z, Magyar C, Tusnády G, Simon I (2003) SCide: identification of stabilization centers in proteins. Bioinformatics 19: 899-900.
    • (2003) Bioinformatics , vol.19 , pp. 899-900
    • Dosztányi, Z.1    Magyar, C.2    Tusnády, G.3    Simon, I.4
  • 11
    • 0031551577 scopus 로고    scopus 로고
    • Stabilization centers in proteins: Identification, characterization and predictions
    • Dosztányi Z, Fiser A, Simon I (1997) Stabilization centers in proteins: identification, characterization and predictions. J Mol Biol 272: 597-612.
    • (1997) J Mol Biol , vol.272 , pp. 597-612
    • Dosztányi, Z.1    Fiser, A.2    Simon, I.3
  • 14
    • 12844284527 scopus 로고    scopus 로고
    • The N-terminal to C-terminal motif in protein folding and function
    • Krishna MM, Englander SW (2005) The N-terminal to C-terminal motif in protein folding and function. Proc Natl Acad Sci U S A 102: 1053-1058.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 1053-1058
    • Krishna, M.M.1    Englander, S.W.2
  • 15
    • 0031791519 scopus 로고    scopus 로고
    • Proteolysis as a measure of the free energy difference between cytochrome c and its derivatives
    • Wang L, Kallenbach NR (1998) Proteolysis as a measure of the free energy difference between cytochrome c and its derivatives. Protein Sci 7: 2460-2464.
    • (1998) Protein Sci , vol.7 , pp. 2460-2464
    • Wang, L.1    Kallenbach, N.R.2
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 78651163419 scopus 로고
    • Disc Electrophoresis. I. Background and theory
    • Ornstein L, Davis BJ (1964) Disc Electrophoresis. I. Background and theory. Ann N Y Acad Sci 121: 321-349.
    • (1964) Ann N Y Acad Sci , vol.121 , pp. 321-349
    • Ornstein, L.1    Davis, B.J.2
  • 18
    • 18744391410 scopus 로고    scopus 로고
    • Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding
    • Park C, Marqusee S (2005) Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding. Nat Methods 2(3): 207-212.
    • (2005) Nat Methods , vol.2 , Issue.3 , pp. 207-212
    • Park, C.1    Marqusee, S.2
  • 19
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC (2003) SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res 31: 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 20
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb Viewer: An environment for the comparative protein modeling
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-Pdb Viewer: an environment for the comparative protein modeling. Electrophoresis 18: 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 21
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the Accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz R, Braun W (1998) Exact and efficient analytical calculation of the Accessible surface areas and their gradients for macromolecules. J Comp Chem 19: 319-333.
    • (1998) J Comp Chem , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 22
    • 0029018048 scopus 로고
    • Cloning and DNA Sequencing of xyaA, a gene encoding an endo-beta-1,4-xylanase from an alkalophilic Bacillus strain (N137)
    • Tabernero C, Sánchez-Torres J, Pérez P, Santamaría RI (1995) Cloning and DNA Sequencing of xyaA, a gene encoding an endo-beta-1,4-xylanase from an alkalophilic Bacillus strain (N137). Appl Environ Microbiol 61: 2420-2424.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2420-2424
    • Tabernero, C.1    Sánchez-Torres, J.2    Pérez, P.3    Santamaría, R.I.4
  • 23
    • 33745698009 scopus 로고    scopus 로고
    • Cloning, sequencing analysis and expression of a gene encoding an endoxylanase from Bacillus halodurans S7
    • Mamo G, Delgado O, Martinez A, Mattiasson B, Kaul RJ (2006) Cloning, sequencing analysis and expression of a gene encoding an endoxylanase from Bacillus halodurans S7. Mol Biotechnol 33: 149-159.
    • (2006) Mol Biotechnol , vol.33 , pp. 149-159
    • Mamo, G.1    Delgado, O.2    Martinez, A.3    Mattiasson, B.4    Kaul, R.J.5
  • 24
    • 2942532539 scopus 로고    scopus 로고
    • Cloning and characterization of two thermostable xylanases from an alkaliphilic Bacillus firmus
    • Chang P, Tsai WS, Tsai CL, Tseng MJ (2004) Cloning and characterization of two thermostable xylanases from an alkaliphilic Bacillus firmus. Biochem Biophys Res Commun 319: 1017-1025.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 1017-1025
    • Chang, P.1    Tsai, W.S.2    Tsai, C.L.3    Tseng, M.J.4
  • 25
    • 0024490818 scopus 로고
    • Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo
    • Luger K, Hommel U, Herold M, Hofsteenge J, Kirschner K (1989) Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo. Science 243: 206-210.
    • (1989) Science , vol.243 , pp. 206-210
    • Luger, K.1    Hommel, U.2    Herold, M.3    Hofsteenge, J.4    Kirschner, K.5
  • 26
    • 0026584311 scopus 로고
    • Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: Indoleglycerolphosphate synthase from Escherichia coli refined at 2.0A resolution
    • Wilmanns M, Priestle JP, Niermann T, Jansonius JN (1992) Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0A resolution. J Mol Biol 223: 477-507.
    • (1992) J Mol Biol , vol.223 , pp. 477-507
    • Wilmanns, M.1    Priestle, J.P.2    Niermann, T.3    Jansonius, J.N.4
  • 27
    • 0028994307 scopus 로고    scopus 로고
    • 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
    • Hennig M, Darimont B, Sterner R, Kirschner K, Jansonius JN (1995) 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure 3: 1295-1306.
    • Structure , vol.3 , pp. 1295-1306
    • Hennig, M.1    Darimont, B.2    Sterner, R.3    Kirschner, K.4    Jansonius, J.N.5
  • 28
    • 0037041035 scopus 로고
    • The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges
    • Knöchel T, Pappenberger A, Jansonius JN, Kirschner K (1995) The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges. J Biol Chem 277: 8626-8634.
    • (1995) J Biol Chem , vol.277 , pp. 8626-8634
    • Knöchel, T.1    Pappenberger, A.2    Jansonius, J.N.3    Kirschner, K.4
  • 29
    • 33745273597 scopus 로고    scopus 로고
    • Probing the structural basis for the difference in thermostability displayed by family 10 xylanases
    • Xie H, Flint J, Vardakou M, Lakey JH, Lewis RJ, et al. (2006) Probing the structural basis for the difference in thermostability displayed by family 10 xylanases. J Mol Biol 360: 157-167.
    • (2006) J Mol Biol , vol.360 , pp. 157-167
    • Xie, H.1    Flint, J.2    Vardakou, M.3    Lakey, J.H.4    Lewis, R.J.5
  • 30
    • 0343293808 scopus 로고    scopus 로고
    • An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: Structural basis and molecular study
    • Georis J, De Lemos Esteves F, Lamotte-Brasseur J, Bougnet V, Devreese B, et al. (2000) An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: structural basis and molecular study. Protein Sci 9: 466-475.
    • (2000) Protein Sci , vol.9 , pp. 466-475
    • Georis, J.1    de Lemos Esteves, F.2    Lamotte-Brasseur, J.3    Bougnet, V.4    Devreese, B.5
  • 31
    • 0037223885 scopus 로고    scopus 로고
    • Aromatic stacking as a determinant of the thermal stability of CYP119 from Sulfolobus solfataricus
    • Puchkaev AV, Koo LS, Ortiz de Montellano PR (2003) Aromatic stacking as a determinant of the thermal stability of CYP119 from Sulfolobus solfataricus. Arch Biochem Biophy 409: 52-58.
    • (2003) Arch Biochem Biophy , vol.409 , pp. 52-58
    • Puchkaev, A.V.1    Koo, L.S.2    Ortiz de Montellano, P.R.3
  • 32
    • 21044446997 scopus 로고    scopus 로고
    • Structural basis for thermostability of endo-1,5-alpha-L- arabinanase from Bacillus thermodenitrificans TS-3
    • Yamaguchi A, Tada T, Wada K, Nakaniwa T, Kitatani T, et al. (2005) Structural basis for thermostability of endo-1,5-alpha-L- arabinanase from Bacillus thermodenitrificans TS-3. J Biochem 137: 587-592.
    • (2005) J Biochem , vol.137 , pp. 587-592
    • Yamaguchi, A.1    Tada, T.2    Wada, K.3    Nakaniwa, T.4    Kitatani, T.5
  • 34
    • 0033773555 scopus 로고    scopus 로고
    • Role of a solvent-exposed aromatic cluster in the folding of Escherichia coli CspA
    • Rodriguez HM, Vu DM, Gregoret LM (2000) Role of a solvent-exposed aromatic cluster in the folding of Escherichia coli CspA. Protein Sci 9: 1993-2000.
    • (2000) Protein Sci , vol.9 , pp. 1993-2000
    • Rodriguez, H.M.1    Vu, D.M.2    Gregoret, L.M.3
  • 35
    • 1842532028 scopus 로고    scopus 로고
    • Locating the stabilizing residues in (alpha/beta)8 barrel proteins based on hydrophobicity, long-range interactions, and sequence conservation
    • Gromiha MM, Pujadas G, Magyar C, Selvaraj S, Simon I (2004) Locating the stabilizing residues in (alpha/beta)8 barrel proteins based on hydrophobicity, long-range interactions, and sequence conservation. Proteins 55: 316-329.
    • (2004) Proteins , vol.55 , pp. 316-329
    • Gromiha, M.M.1    Pujadas, G.2    Magyar, C.3    Selvaraj, S.4    Simon, I.5
  • 36
    • 28644442880 scopus 로고    scopus 로고
    • Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8
    • Ihsanawati KT, Kaneko T, Morokuma C, Yatsunami R, Sato T, et al. (2005) Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8. Proteins 61: 999-1009.
    • (2005) Proteins , vol.61 , pp. 999-1009
    • Ihsanawati, K.T.1    Kaneko, T.2    Morokuma, C.3    Yatsunami, R.4    Sato, T.5
  • 37
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson FM, Wright PE, Baldwin RL (1990) Structural characterization of a partly folded apomyoglobin intermediate. Science 249: 1544-1548.
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 38
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings PA, Wright PE (1993) Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262: 892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 39
    • 0033514920 scopus 로고    scopus 로고
    • Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate
    • Kay MS, Ramos CH, Baldwin RL (1999) Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate. Proc Natl Acad Sci U S A 96: 2007-2012.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 2007-2012
    • Kay, M.S.1    Ramos, C.H.2    Baldwin, R.L.3
  • 40
    • 0034727682 scopus 로고    scopus 로고
    • Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions
    • Funahashi J, Tkano K, Yamagata Y, Yutani K (2000) Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. Biochemistry 39(47): 14448-14456.
    • (2000) Biochemistry , vol.39 , Issue.47 , pp. 14448-14456
    • Funahashi, J.1    Tkano, K.2    Yamagata, Y.3    Yutani, K.4
  • 41
    • 0025317840 scopus 로고
    • Reverse hydrophobic effects relieved by amino acid substitutions at a protein surface
    • Pakula AA, Sauer RT (1990) Reverse hydrophobic effects relieved by amino acid substitutions at a protein surface. Nature 344(6264): 363-364.
    • (1990) Nature , vol.344 , Issue.6264 , pp. 363-364
    • Pakula, A.A.1    Sauer, R.T.2
  • 42
    • 0034100848 scopus 로고    scopus 로고
    • Two exposed amino acid residues confer thermostability on a cold shock protein
    • Perl D, Mueller U, Heinemann U, Schmid FX (2000) Two exposed amino acid residues confer thermostability on a cold shock protein. Nature 7(5): 380-383.
    • (2000) Nature , vol.7 , Issue.5 , pp. 380-383
    • Perl, D.1    Mueller, U.2    Heinemann, U.3    Schmid, F.X.4
  • 43
    • 0032032172 scopus 로고    scopus 로고
    • Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis
    • Schindler T, Perl D, Graumann P, Sieber V, Marahiel MA, et al. (1998) Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. Proteins Struct Func Genet 30: 401-406.
    • (1998) Proteins Struct Func Genet , vol.30 , pp. 401-406
    • Schindler, T.1    Perl, D.2    Graumann, P.3    Sieber, V.4    Marahiel, M.A.5
  • 44
    • 0037837789 scopus 로고    scopus 로고
    • Kinetic Stabilization of Bacillus licheniformis a-Amylase through Introduction of Hydrophobic Residues at the Surface
    • Machius M, Declerck N, Huber R, Wiegand G (2003) Kinetic Stabilization of Bacillus licheniformis a-Amylase through Introduction of Hydrophobic Residues at the Surface. J Biol Chem 278: 11546-11553.
    • (2003) J Biol Chem , vol.278 , pp. 11546-11553
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 45
    • 0031591389 scopus 로고    scopus 로고
    • The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: Structural characterization of proline-substitution sites for protein thermostabilization
    • Watanabe K, Hata Y, Kizaki H, Katsube Y, Suzuki Y (1997) The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization. J Mol Biol 269: 142-153.
    • (1997) J Mol Biol , vol.269 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5
  • 46
    • 1542782097 scopus 로고    scopus 로고
    • In Vitro Protein Complex Formation with Cytoskeleton-anchoring Domain of Occludin Identified by Limited Proteolysis
    • Peng B-H, Lee JC, Campbell GA (2003) In Vitro Protein Complex Formation with Cytoskeleton-anchoring Domain of Occludin Identified by Limited Proteolysis. J Biol Chem 278: 49644-49651.
    • (2003) J Biol Chem , vol.278 , pp. 49644-49651
    • Peng, B.-H.1    Lee, J.C.2    Campbell, G.A.3
  • 47
    • 0037592332 scopus 로고    scopus 로고
    • Glutamate Receptor Subunit 3 Is Modified by Sitespecific Limited Proteolysis Including Cleavage by?-Secretase
    • Meyer EL, Strutz N, Gahring LC, Rogers SW (2003) Glutamate Receptor Subunit 3 Is Modified by Sitespecific Limited Proteolysis Including Cleavage by?-Secretase. J Biol Chem 278: 23786-23796.
    • (2003) J Biol Chem , vol.278 , pp. 23786-23796
    • Meyer, E.L.1    Strutz, N.2    Gahring, L.C.3    Rogers, S.W.4
  • 48
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I, Berger A (1967) On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 27: 157-162.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2


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