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Volumn 11, Issue SUPPL. 6, 2010, Pages

Enzyme structure dynamics of xylanase I from Trichoderma longibrachiatum

Author keywords

[No Author keywords available]

Indexed keywords

CELL WALL-DEGRADING ENZYMES; HYDROGEN-DEUTERIUM EXCHANGE; MASS SPECTROMETRY ANALYSIS; MOLECULAR MECHANISM; REGIONAL STRUCTURE; STRUCTURE-FUNCTION RELATIONSHIP; THREE-DIMENSIONAL STRUCTURE; TRICHODERMA LONGIBRACHIATUM;

EID: 77957698074     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-11-12     Document Type: Article
Times cited : (8)

References (41)
  • 1
    • 0030892096 scopus 로고    scopus 로고
    • Cloning and sequence analysis of genes encoding xylanases and acetyl xylan esterase from Streptomyces thermomviolaceus OPC-520.
    • 168356, 9023944
    • Tsujibo H, Ohtsuki T, Iio T, Yamazaki I, Miyamoto K, Sugiyama M, Inamori Y. Cloning and sequence analysis of genes encoding xylanases and acetyl xylan esterase from Streptomyces thermomviolaceus OPC-520. Appl. Environ Microbiol 1997, 63:661-664. 168356, 9023944.
    • (1997) Appl. Environ Microbiol , vol.63 , pp. 661-664
    • Tsujibo, H.1    Ohtsuki, T.2    Iio, T.3    Yamazaki, I.4    Miyamoto, K.5    Sugiyama, M.6    Inamori, Y.7
  • 2
    • 71749113628 scopus 로고    scopus 로고
    • Thermostable carbohydrate binding module increases the thermostability and substrate-binding capacity of Trichoderma reesei xylanase 2.
    • Jun H, Bing Y, Keying Z, Xuemei D, Daiwen C. Thermostable carbohydrate binding module increases the thermostability and substrate-binding capacity of Trichoderma reesei xylanase 2. New Biotech 2009, 26:53-59.
    • (2009) New Biotech , vol.26 , pp. 53-59
    • Jun, H.1    Bing, Y.2    Keying, Z.3    Xuemei, D.4    Daiwen, C.5
  • 3
    • 38949210848 scopus 로고    scopus 로고
    • Enzyme improvement in the absence of structural knowledge: a novel statistical approach.
    • Barak Y, Nov Y, Ackerley DF, Matin A. Enzyme improvement in the absence of structural knowledge: a novel statistical approach. The ĪSME J 2008, 2:171-179.
    • (2008) The ĪSME J , vol.2 , pp. 171-179
    • Barak, Y.1    Nov, Y.2    Ackerley, D.F.3    Matin, A.4
  • 4
    • 77957702169 scopus 로고
    • Darwin's dangerous idea: Evolution and the meanings of life.
    • New York, NY
    • Dennett DC. Darwin's dangerous idea: Evolution and the meanings of life. Simon & Schuster Inc 1995, New York, NY.
    • (1995) Simon & Schuster Inc
    • Dennett, D.C.1
  • 5
    • 29544433799 scopus 로고    scopus 로고
    • Directed evolution of metabolic pathways.
    • Chatterjee R, Yuan L. Directed evolution of metabolic pathways. Trends Biotech 2006, 24:28-38.
    • (2006) Trends Biotech , vol.24 , pp. 28-38
    • Chatterjee, R.1    Yuan, L.2
  • 6
    • 33644851164 scopus 로고    scopus 로고
    • Fancy footwork in the sequence space shuffle.
    • Arnold FH. Fancy footwork in the sequence space shuffle. Nat Biotech 2006, 24:328-330.
    • (2006) Nat Biotech , vol.24 , pp. 328-330
    • Arnold, F.H.1
  • 7
    • 27544462342 scopus 로고    scopus 로고
    • Role of protein dynamics in reaction rate enhancement by enzymes.
    • 10.1021/ja055251s, 16248667
    • Agarwal PK. Role of protein dynamics in reaction rate enhancement by enzymes. J Am Chem Soc 2005, 127(43):15248-15256. 10.1021/ja055251s, 16248667.
    • (2005) J Am Chem Soc , vol.127 , Issue.43 , pp. 15248-15256
    • Agarwal, P.K.1
  • 8
    • 33644559358 scopus 로고    scopus 로고
    • Enzymes: An integrated view of structure, dynamics and function.
    • 10.1186/1475-2859-5-2, 1379655, 16409630
    • Agarwal PK. Enzymes: An integrated view of structure, dynamics and function. Microb Cell Fact 2006, 5. 10.1186/1475-2859-5-2, 1379655, 16409630.
    • (2006) Microb Cell Fact , vol.5
    • Agarwal, P.K.1
  • 9
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins.
    • 10.1038/nature06522, 18075575
    • Henzler-Wildman K, Kern D. Dynamic personalities of proteins. Nature 2007, 450(7172):964-972. 10.1038/nature06522, 18075575.
    • (2007) Nature , vol.450 , Issue.7172 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 10
    • 33748777424 scopus 로고    scopus 로고
    • Enzyme conformational dynamics during catalysis and in the 'resting state' monitored by hydrogen/deuterium exchange mass spectrometry.
    • 10.1016/j.febslet.2006.08.042, 16963025
    • Liu YH, Konermann L. Enzyme conformational dynamics during catalysis and in the 'resting state' monitored by hydrogen/deuterium exchange mass spectrometry. FEBS Lett 2006, 580(22):5137-5142. 10.1016/j.febslet.2006.08.042, 16963025.
    • (2006) FEBS Lett , vol.580 , Issue.22 , pp. 5137-5142
    • Liu, Y.H.1    Konermann, L.2
  • 12
    • 0041852853 scopus 로고    scopus 로고
    • The role of dynamics in enzyme activity.
    • 10.1146/annurev.biophys.32.110601.142445, 12471064
    • Daniel RM, Dunn RV, Finney JL, Smith JC. The role of dynamics in enzyme activity. Annu Rev Biophys Biomol Struct 2003, 32:69-92. 10.1146/annurev.biophys.32.110601.142445, 12471064.
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 69-92
    • Daniel, R.M.1    Dunn, R.V.2    Finney, J.L.3    Smith, J.C.4
  • 13
    • 0037154884 scopus 로고    scopus 로고
    • Enzyme dynamics during catalysis.
    • 10.1126/science.1066176, 11859194
    • Eisenmesser EZ, Bosco DA, Akke M, Kern D. Enzyme dynamics during catalysis. Science 2002, 295(5559):1520-1523. 10.1126/science.1066176, 11859194.
    • (2002) Science , vol.295 , Issue.5559 , pp. 1520-1523
    • Eisenmesser, E.Z.1    Bosco, D.A.2    Akke, M.3    Kern, D.4
  • 14
    • 33746325760 scopus 로고    scopus 로고
    • Relating protein motion to catalysis.
    • 10.1146/annurev.biochem.75.103004.142800, 16756501
    • Hammes-Schiffer S, Benkovic SJ. Relating protein motion to catalysis. Annu Rev Biochem 2006, 75:519-541. 10.1146/annurev.biochem.75.103004.142800, 16756501.
    • (2006) Annu Rev Biochem , vol.75 , pp. 519-541
    • Hammes-Schiffer, S.1    Benkovic, S.J.2
  • 15
    • 0037214137 scopus 로고    scopus 로고
    • Protein hydrogen exchange mechanism: local fluctuations.
    • 10.1110/ps.0225803, 2312409, 12493838
    • Maity H, Lim WK, Rumbley JN, Englander SW. Protein hydrogen exchange mechanism: local fluctuations. Protein Sci 2003, 12(1):153-160. 10.1110/ps.0225803, 2312409, 12493838.
    • (2003) Protein Sci , vol.12 , Issue.1 , pp. 153-160
    • Maity, H.1    Lim, W.K.2    Rumbley, J.N.3    Englander, S.W.4
  • 16
    • 33144462544 scopus 로고    scopus 로고
    • Probing protein ligand interactions by automated hydrogen/deuterium exchange mass spectrometry.
    • 10.1021/ac051294f, 16478090
    • Chalmers MJ, Busby SA, Pascal BD, He Y, Hendrickson CL, Marshall AG, Griffin PR. Probing protein ligand interactions by automated hydrogen/deuterium exchange mass spectrometry. Anal Chem 2006, 78(4):1005-1014. 10.1021/ac051294f, 16478090.
    • (2006) Anal Chem , vol.78 , Issue.4 , pp. 1005-1014
    • Chalmers, M.J.1    Busby, S.A.2    Pascal, B.D.3    He, Y.4    Hendrickson, C.L.5    Marshall, A.G.6    Griffin, P.R.7
  • 17
    • 33144487234 scopus 로고    scopus 로고
    • Roles of static and dynamic domains in stability and catalysis of adenylate kinase.
    • 10.1073/pnas.0507527103, 1413696, 16452168
    • Bae E, Phillips GN. Roles of static and dynamic domains in stability and catalysis of adenylate kinase. Proc Natl Acad Sci U S A 2006, 103(7):2132-2137. 10.1073/pnas.0507527103, 1413696, 16452168.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.7 , pp. 2132-2137
    • Bae, E.1    Phillips, G.N.2
  • 18
    • 49549086897 scopus 로고    scopus 로고
    • Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches.
    • Konermann L, Tong X, Pan Y. Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches. J. Mass Spec 2008, 43:1021-1036.
    • (2008) J. Mass Spec , vol.43 , pp. 1021-1036
    • Konermann, L.1    Tong, X.2    Pan, Y.3
  • 20
    • 33644663381 scopus 로고    scopus 로고
    • Folding kinetics of the S100A11 protein dimer studied by time-resolved electrospray mass spectrometry and pulsed hydrogen-deuterium exchange.
    • 10.1021/bi052349a, 16503655
    • Pan JX, Rintala-Dempsey A, Li Y, Shaw GS, Konermann L. Folding kinetics of the S100A11 protein dimer studied by time-resolved electrospray mass spectrometry and pulsed hydrogen-deuterium exchange. Biochemistry 2006, 45:3005. 10.1021/bi052349a, 16503655.
    • (2006) Biochemistry , vol.45 , pp. 3005
    • Pan, J.X.1    Rintala-Dempsey, A.2    Li, Y.3    Shaw, G.S.4    Konermann, L.5
  • 21
    • 3342925849 scopus 로고    scopus 로고
    • Methods to study protein dynamics and folding by mass spectrometry.
    • 10.1016/j.ymeth.2004.03.015, 15283918
    • Eyles SJ, Kaltashov IA. Methods to study protein dynamics and folding by mass spectrometry. Methods 2004, 34:88. 10.1016/j.ymeth.2004.03.015, 15283918.
    • (2004) Methods , vol.34 , pp. 88
    • Eyles, S.J.1    Kaltashov, I.A.2
  • 22
    • 0027770910 scopus 로고
    • Detection of transient protein folding populations by mass spectrometry.
    • 10.1126/science.8235611, 8235611
    • Miranker A, Robinson CV, Radford SE, Aplin R, Dobson CM. Detection of transient protein folding populations by mass spectrometry. Science 1993, 262:896. 10.1126/science.8235611, 8235611.
    • (1993) Science , vol.262 , pp. 896
    • Miranker, A.1    Robinson, C.V.2    Radford, S.E.3    Aplin, R.4    Dobson, C.M.5
  • 23
    • 0037019523 scopus 로고    scopus 로고
    • A general mass spectrometry-based assay for the quantitation of protein-ligand binding interactions in solution.
    • 10.1021/ja026574g, 12197709
    • Powell KD, Ghaemmaghami S, Wang MZ, Ma L, Oas TG, Fitzgerald MC. A general mass spectrometry-based assay for the quantitation of protein-ligand binding interactions in solution. J Am Chem Soc 2002, 124:10256-10257. 10.1021/ja026574g, 12197709.
    • (2002) J Am Chem Soc , vol.124 , pp. 10256-10257
    • Powell, K.D.1    Ghaemmaghami, S.2    Wang, M.Z.3    Ma, L.4    Oas, T.G.5    Fitzgerald, M.C.6
  • 24
    • 37549005981 scopus 로고    scopus 로고
    • Vibrid cholerae toxin-coregulated pilus structure analyzed by hydrogen/deuterium exchange mass spectrometry.
    • 10.1016/j.str.2007.10.027, 2238685, 18184591
    • Li J, Lim MS, Li S, Brock M, Pique ME, Woods VL, Craig L. Vibrid cholerae toxin-coregulated pilus structure analyzed by hydrogen/deuterium exchange mass spectrometry. Structure 2008, 16(1):137-148. 10.1016/j.str.2007.10.027, 2238685, 18184591.
    • (2008) Structure , vol.16 , Issue.1 , pp. 137-148
    • Li, J.1    Lim, M.S.2    Li, S.3    Brock, M.4    Pique, M.E.5    Woods, V.L.6    Craig, L.7
  • 25
    • 36148991818 scopus 로고    scopus 로고
    • Conformational analysis of Epac activation using amide hydrogen/deuterium exchange mass Spectrometry.
    • 10.1074/jbc.M706231200, 17785454
    • Brock M, Fan F, Mei FC, Li S, Gessner C, Woods VL, Cheng X. Conformational analysis of Epac activation using amide hydrogen/deuterium exchange mass Spectrometry. J Biol Chem 2007, 282(44):32256-32263. 10.1074/jbc.M706231200, 17785454.
    • (2007) J Biol Chem , vol.282 , Issue.44 , pp. 32256-32263
    • Brock, M.1    Fan, F.2    Mei, F.C.3    Li, S.4    Gessner, C.5    Woods, V.L.6    Cheng, X.7
  • 27
    • 3342925849 scopus 로고    scopus 로고
    • Methods to study protein dynamics and folding by mass spectrometry.
    • 10.1016/j.ymeth.2004.03.015, 15283918
    • Eyles SJ, Kaltashov IA. Methods to study protein dynamics and folding by mass spectrometry. Methods 2004, 34(1):88-99. 10.1016/j.ymeth.2004.03.015, 15283918.
    • (2004) Methods , vol.34 , Issue.1 , pp. 88-99
    • Eyles, S.J.1    Kaltashov, I.A.2
  • 28
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: A historical perspective.
    • Englander SW. Hydrogen exchange and mass spectrometry: A historical perspective. J Am Soc Mass Spectrom 2006,
    • (2006) J Am Soc Mass Spectrom
    • Englander, S.W.1
  • 29
    • 32244447012 scopus 로고    scopus 로고
    • Molecular basis for substrate recognition by MTMR2, a myotubularin family phosphoinositide phosphatase.
    • 10.1073/pnas.0510006103, 1347996, 16410353
    • Begley MJ, Taylor GS, Brock MA, Ghosh P, Woods VL, Dixon JE. Molecular basis for substrate recognition by MTMR2, a myotubularin family phosphoinositide phosphatase. Proc Natl Acad Sci U S A 2006, 103(4):927-932. 10.1073/pnas.0510006103, 1347996, 16410353.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.4 , pp. 927-932
    • Begley, M.J.1    Taylor, G.S.2    Brock, M.A.3    Ghosh, P.4    Woods, V.L.5    Dixon, J.E.6
  • 30
    • 29344436799 scopus 로고    scopus 로고
    • Molecular determinants for interaction of SHEP1 with Cas localize to a highly solvent-protected region in the complex.
    • 10.1016/j.febslet.2005.11.070, 16364304
    • Derunes C, Burgess R, Iraheta E, Kellerer R, Becherer K, Gessner CR, Li S, Hewitt K, Vuori K, Pasquale EB. Molecular determinants for interaction of SHEP1 with Cas localize to a highly solvent-protected region in the complex. FEBS Lett 2006, 580(1):175-178. 10.1016/j.febslet.2005.11.070, 16364304.
    • (2006) FEBS Lett , vol.580 , Issue.1 , pp. 175-178
    • Derunes, C.1    Burgess, R.2    Iraheta, E.3    Kellerer, R.4    Becherer, K.5    Gessner, C.R.6    Li, S.7    Hewitt, K.8    Vuori, K.9    Pasquale, E.B.10
  • 31
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.
    • 10.1038/335700a0, 2845279
    • Roder H, Elove GA, Englander SW. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature 1988, 335(6192):700-704. 10.1038/335700a0, 2845279.
    • (1988) Nature , vol.335 , Issue.6192 , pp. 700-704
    • Roder, H.1    Elove, G.A.2    Englander, S.W.3
  • 32
    • 3242884785 scopus 로고    scopus 로고
    • Structural determinants for generating centromeric chromatin.
    • 10.1038/nature02766, 15282608
    • Black BE, Foltz DR, Chakravarthy S, Luger K, Woods VL, Cleveland DW. Structural determinants for generating centromeric chromatin. Nature 2004, 430(6999):578-582. 10.1038/nature02766, 15282608.
    • (2004) Nature , vol.430 , Issue.6999 , pp. 578-582
    • Black, B.E.1    Foltz, D.R.2    Chakravarthy, S.3    Luger, K.4    Woods, V.L.5    Cleveland, D.W.6
  • 33
    • 1842558963 scopus 로고    scopus 로고
    • High-throughput screening assay for the tunable selection of protein ligands.
    • Powell KD, Fitzgerald MC. High-throughput screening assay for the tunable selection of protein ligands. J Combin Chem 2004, 6(2):262-269.
    • (2004) J Combin Chem , vol.6 , Issue.2 , pp. 262-269
    • Powell, K.D.1    Fitzgerald, M.C.2
  • 34
    • 23644439447 scopus 로고    scopus 로고
    • Catalytic independent functions of a protein kinase as revealed by a kinase-dead mutant: Study of the Lys72 His mutant of cAMP-dependent kinase.
    • 10.1016/j.jmb.2005.06.011, 16054648
    • Iyer GH, Garrod S, Woods VL, Taylor SS. Catalytic independent functions of a protein kinase as revealed by a kinase-dead mutant: Study of the Lys72 His mutant of cAMP-dependent kinase. J Mol Biol 2005, 351(5):1110-1122. 10.1016/j.jmb.2005.06.011, 16054648.
    • (2005) J Mol Biol , vol.351 , Issue.5 , pp. 1110-1122
    • Iyer, G.H.1    Garrod, S.2    Woods, V.L.3    Taylor, S.S.4
  • 35
    • 0042279172 scopus 로고    scopus 로고
    • Protein analysis by hydrogen exchange mass spectrometry.
    • 10.1146/annurev.biophys.32.110601.142417, 12598366
    • Hoofnagle AN, Resing KA, Ahn NG. Protein analysis by hydrogen exchange mass spectrometry. Annu Rev Biophys Biomol Struct 2003, 32:1-25. 10.1146/annurev.biophys.32.110601.142417, 12598366.
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 1-25
    • Hoofnagle, A.N.1    Resing, K.A.2    Ahn, N.G.3
  • 36
    • 0029046847 scopus 로고
    • Electrospray mass spectrometry for protein characterization.
    • 10.1016/S0968-0004(00)89019-2, 7631418
    • Mann M, Wilm M. Electrospray mass spectrometry for protein characterization. Trends Biochem Sci 1995, 20(6):219-224. 10.1016/S0968-0004(00)89019-2, 7631418.
    • (1995) Trends Biochem Sci , vol.20 , Issue.6 , pp. 219-224
    • Mann, M.1    Wilm, M.2
  • 37
    • 49549086897 scopus 로고    scopus 로고
    • Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches.
    • Konermann L, Tong X, Pan Y. Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches. J Mass Spec 2008, 43:1021-1036.
    • (2008) J Mass Spec , vol.43 , pp. 1021-1036
    • Konermann, L.1    Tong, X.2    Pan, Y.3
  • 38
    • 0028911057 scopus 로고
    • Structural comparison two major endo-1,4-xylanases from Trichoderma reesei,
    • 10.1021/bi00003a019, 7827044
    • Torronen A, Rouvinen J. Structural comparison two major endo-1,4-xylanases from Trichoderma reesei,. Biochemistry 1995, 34:847-856. 10.1021/bi00003a019, 7827044.
    • (1995) Biochemistry , vol.34 , pp. 847-856
    • Torronen, A.1    Rouvinen, J.2
  • 40
    • 70350050562 scopus 로고    scopus 로고
    • Unique ligand binding patterns between estrogen receptor alpha and beta revealed by hydrogen-deuterium exchange.
    • 10.1021/bi901149t, 19739677
    • Dai SY, Burris PT, Dodge JA, Montrose-Rafizadeh C, Wang Y, Pascal BD, Chalmers MJ, Griffin PR. Unique ligand binding patterns between estrogen receptor alpha and beta revealed by hydrogen-deuterium exchange. Biochemistry 2009, 48(40):9668-9676. 10.1021/bi901149t, 19739677.
    • (2009) Biochemistry , vol.48 , Issue.40 , pp. 9668-9676
    • Dai, S.Y.1    Burris, P.T.2    Dodge, J.A.3    Montrose-Rafizadeh, C.4    Wang, Y.5    Pascal, B.D.6    Chalmers, M.J.7    Griffin, P.R.8
  • 41
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange.
    • 10.1002/prot.340170110, 8234246
    • Bai Y, Milne JS, Mayne L, Englander SW. Primary structure effects on peptide group hydrogen exchange. Proteins 1993, 17(1):75-86. 10.1002/prot.340170110, 8234246.
    • (1993) Proteins , vol.17 , Issue.1 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4


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