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Volumn 290, Issue 38, 2015, Pages 22955-22969

Structural and functional characterization of a lytic polysaccharide monooxygenase with broad substrate specificity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; BINS; CELLULOSE; CRYSTAL STRUCTURE; POLYSACCHARIDES;

EID: 84942879811     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.660183     Document Type: Article
Times cited : (170)

References (57)
  • 4
    • 84055197660 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa
    • Phillips, C. M., Beeson, W. T., Cate, J. H., and Marletta, M. A. (2011) Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. ACS Chem. Biol. 6, 1399-1406
    • (2011) ACS Chem. Biol , vol.6 , pp. 1399-1406
    • Phillips, C.M.1    Beeson, W.T.2    Cate, J.H.3    Marletta, M.A.4
  • 6
    • 77957727454 scopus 로고    scopus 로고
    • An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides
    • Vaaje-Kolstad, G., Westereng, B., Horn, S. J., Liu, Z., Zhai, H., Sørlie, M., and Eijsink, V. G. (2010) An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 330, 219-222
    • (2010) Science , vol.330 , pp. 219-222
    • Vaaje-Kolstad, G.1    Westereng, B.2    Horn, S.J.3    Liu, Z.4    Zhai, H.5    Sørlie, M.6    Eijsink, V.G.7
  • 7
    • 84869205445 scopus 로고    scopus 로고
    • NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions
    • Aachmann, F. L., Sørlie, M., Skjåk-Bræk, G., Eijsink, V. G., and Vaaje-Kolstad, G. (2012) NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions. Proc. Natl. Acad. Sci. U.S.A. 109, 18779-18784
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 18779-18784
    • Aachmann, F.L.1    Sørlie, M.2    Skjåk-Bræk, G.3    Eijsink, V.G.4    Vaaje-Kolstad, G.5
  • 8
    • 84855912007 scopus 로고    scopus 로고
    • Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases
    • Beeson, W. T., Phillips, C. M., Cate, J. H., and Marletta, M. A. (2012) Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases. J. Am. Chem. Soc. 134, 890-892
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 890-892
    • Beeson, W.T.1    Phillips, C.M.2    Cate, J.H.3    Marletta, M.A.4
  • 10
    • 81755178934 scopus 로고    scopus 로고
    • Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61
    • Langston, J. A., Shaghasi, T., Abbate, E., Xu, F., Vlasenko, E., and Sweeney, M. D. (2011) Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61. Appl. Environ. Microbiol. 77, 7007-7015
    • (2011) Appl. Environ. Microbiol , vol.77 , pp. 7007-7015
    • Langston, J.A.1    Shaghasi, T.2    Abbate, E.3    Xu, F.4    Vlasenko, E.5    Sweeney, M.D.6
  • 11
    • 84885472701 scopus 로고    scopus 로고
    • Recent insights into copper-containing lytic polysaccharide mono-oxygenases
    • Hemsworth, G. R., Davies, G. J., and Walton, P. H. (2013) Recent insights into copper-containing lytic polysaccharide mono-oxygenases. Curr. Opin. Struct. Biol. 23, 660-668
    • (2013) Curr. Opin. Struct. Biol , vol.23 , pp. 660-668
    • Hemsworth, G.R.1    Davies, G.J.2    Walton, P.H.3
  • 16
    • 84875193804 scopus 로고    scopus 로고
    • Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes
    • Levasseur, A., Drula, E., Lombard, V., Coutinho, P. M., and Henrissat, B. (2013) Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes. Biotechnol. Biofuels 6, 41
    • (2013) Biotechnol. Biofuels , vol.6 , pp. 41
    • Levasseur, A.1    Drula, E.2    Lombard, V.3    Coutinho, P.M.4    Henrissat, B.5
  • 18
    • 84861987031 scopus 로고    scopus 로고
    • Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases
    • Li, X., Beeson, W. T., 4th., Phillips, C. M., Marletta, M. A., and Cate, J. H. (2012) Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases. Structure 20, 1051-1061
    • (2012) Structure , vol.20 , pp. 1051-1061
    • Li, X.1    Beeson, W.T.2    Phillips, C.M.3    Marletta, M.A.4    Cate, J.H.5
  • 19
    • 0031695160 scopus 로고    scopus 로고
    • Solution structure of the cellulose-binding domain of endoglucanase i from Trichoderma reesei and its interaction with cello-oligosaccharides
    • Mattinen, M. L., Linder, M., Drakenberg, T., and Annila, A. (1998) Solution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello-oligosaccharides. Eur. J. Biochem. 256, 279-286
    • (1998) Eur. J. Biochem , vol.256 , pp. 279-286
    • Mattinen, M.L.1    Linder, M.2    Drakenberg, T.3    Annila, A.4
  • 22
    • 84867753151 scopus 로고    scopus 로고
    • Production of four Neurospora crassa lytic polysaccharide monooxygenases in Pichia pastoris monitored by a fluorimetric assay
    • Kittl, R., Kracher, D., Burgstaller, D., Haltrich, D., and Ludwig, R. (2012) Production of four Neurospora crassa lytic polysaccharide monooxygenases in Pichia pastoris monitored by a fluorimetric assay. Biotechnol. Biofuels 5, 79
    • (2012) Biotechnol. Biofuels , vol.5 , pp. 79
    • Kittl, R.1    Kracher, D.2    Burgstaller, D.3    Haltrich, D.4    Ludwig, R.5
  • 26
    • 79953747244 scopus 로고    scopus 로고
    • An introduction to data reduction: Space-group determination, scaling and intensity statistics
    • Evans, P. R. (2011) An introduction to data reduction: space-group determination, scaling and intensity statistics. Acta Crystallogr. D Biol. Crystallogr. 67, 282-292
    • (2011) Acta Crystallogr. D Biol. Crystallogr , vol.67 , pp. 282-292
    • Evans, P.R.1
  • 30
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 32
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/ wARP version 7
    • Langer, G., Cohen, S. X., Lamzin, V. S., and Perrakis, A. (2008) Automated macromolecular model building for X-ray crystallography using ARP/ wARP version 7. Nat. Protoc. 3, 1171-1179
    • (2008) Nat. Protoc , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 34
    • 34547645216 scopus 로고    scopus 로고
    • Insights into Cu(I) exchange in HAH1 using quantum mechanical and molecular simulations
    • Op't Holt, B. T., and Merz, K. M., Jr. (2007) Insights into Cu(I) exchange in HAH1 using quantum mechanical and molecular simulations. Biochemistry 46, 8816-8826
    • (2007) Biochemistry , vol.46 , pp. 8816-8826
    • Op'T Holt, B.T.1    Merz, K.M.2
  • 35
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • Stoll, S., and Schweiger, A. (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J. Magn. Reson. 178, 42-55
    • (2006) J. Magn. Reson , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 36
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., Williston, S., Brandts, J. F., and Lin, L. N. (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179, 131-137
    • (1989) Anal. Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 37
    • 77957061124 scopus 로고
    • Preparation of crystalline, amorphous, and dyed cellulase substrates
    • Wood, T. M. (1988) Preparation of crystalline, amorphous, and dyed cellulase substrates. Methods Enzymol. 160, 19-25
    • (1988) Methods Enzymol , vol.160 , pp. 19-25
    • Wood, T.M.1
  • 38
    • 20344363170 scopus 로고    scopus 로고
    • Determination of the number-average degree of polymerization of cellodextrins and cellulose with application to enzymatic hydrolysis
    • Zhang, Y. H., and Lynd, L. R. (2005) Determination of the number-average degree of polymerization of cellodextrins and cellulose with application to enzymatic hydrolysis. Biomacromolecules 6, 1510-1515
    • (2005) Biomacromolecules , vol.6 , pp. 1510-1515
    • Zhang, Y.H.1    Lynd, L.R.2
  • 39
    • 0034544771 scopus 로고    scopus 로고
    • Use of stopped-flow spectrophotometry to establish midpoint potentials for redox proteins
    • Sørlie, M., Seefeldt, L. C., and Parker, V. D. (2000) Use of stopped-flow spectrophotometry to establish midpoint potentials for redox proteins. Anal. Biochem. 287, 118-125
    • (2000) Anal. Biochem , vol.287 , pp. 118-125
    • Sørlie, M.1    Seefeldt, L.C.2    Parker, V.D.3
  • 40
    • 0031214544 scopus 로고    scopus 로고
    • Entropies of redox reactions between proteins and mediators: The temperature dependence of reversible electrode potentials in aqueous buffers
    • Liu, Y., Seefeldt, L. C., and Parker, V. D. (1997) Entropies of redox reactions between proteins and mediators: the temperature dependence of reversible electrode potentials in aqueous buffers. Anal. Biochem. 250, 196-202
    • (1997) Anal. Biochem , vol.250 , pp. 196-202
    • Liu, Y.1    Seefeldt, L.C.2    Parker, V.D.3
  • 41
    • 84871386903 scopus 로고    scopus 로고
    • Efficient separation of oxidized cello-oligosaccharides generated by cellulose degrading lytic polysaccharide monooxygenases
    • Westereng, B., Agger, J. W., Horn, S. J., Vaaje-Kolstad, G., Aachmann, F. L., Stenstrøm, Y. H., and Eijsink, V. G. (2013) Efficient separation of oxidized cello-oligosaccharides generated by cellulose degrading lytic polysaccharide monooxygenases. J. Chromatogr. A 1271, 144-152
    • (2013) J. Chromatogr. A , vol.1271 , pp. 144-152
    • Westereng, B.1    Agger, J.W.2    Horn, S.J.3    Vaaje-Kolstad, G.4    Aachmann, F.L.5    Stenstrøm, Y.H.6    Eijsink, V.G.7
  • 43
    • 84892745213 scopus 로고    scopus 로고
    • Determinants of regioselective hydroxylation in the fungal polysaccharide monooxygenases
    • Vu, V. V., Beeson, W. T., Phillips, C. M., Cate, J. H., and Marletta, M. A. (2014) Determinants of regioselective hydroxylation in the fungal polysaccharide monooxygenases. J. Am. Chem. Soc. 136, 562-565
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 562-565
    • Vu, V.V.1    Beeson, W.T.2    Phillips, C.M.3    Cate, J.H.4    Marletta, M.A.5
  • 44
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenström, P.2
  • 45
    • 84918563784 scopus 로고    scopus 로고
    • Fungal cellulose degradation by oxidative enzymes: From dysfunctional GH61 family to powerful lytic polysaccharide monooxygenase family
    • Morgenstern, I., Powlowski, J., and Tsang, A. (2014) Fungal cellulose degradation by oxidative enzymes: from dysfunctional GH61 family to powerful lytic polysaccharide monooxygenase family. Brief. Funct. Genomics 13, 471-481
    • (2014) Brief. Funct. Genomics , vol.13 , pp. 471-481
    • Morgenstern, I.1    Powlowski, J.2    Tsang, A.3
  • 46
    • 84898944979 scopus 로고    scopus 로고
    • Comparative study of two chitinactive and two cellulose-active AA10-type lytic polysaccharide monooxygenases
    • Forsberg, Z., Røhr, A. K., Mekasha, S., Andersson, K. K., Eijsink, V. G., Vaaje-Kolstad, G., and Sørlie, M. (2014) Comparative study of two chitinactive and two cellulose-active AA10-type lytic polysaccharide monooxygenases. Biochemistry 53, 1647-1656
    • (2014) Biochemistry , vol.53 , pp. 1647-1656
    • Forsberg, Z.1    Røhr, A.K.2    Mekasha, S.3    Andersson, K.K.4    Eijsink, V.G.5    Vaaje-Kolstad, G.6    Sørlie, M.7
  • 47
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: Can low affinity systems be studied by isothermal titration calorimetry?
    • Turnbull, W. B., and Daranas, A. H. (2003) On the value of c: can low affinity systems be studied by isothermal titration calorimetry? J. Am. Chem. Soc. 125, 14859-14866
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 48
    • 0030589514 scopus 로고    scopus 로고
    • -/-chology: Ramachandran revisited
    • Kleywegt, G. J., and Jones, T. A. (1996)-/-chology: Ramachandran revisited. Structure 4, 1395-1400
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 49
    • 84891926133 scopus 로고    scopus 로고
    • Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism
    • Kim, S., Ståhlberg, J., Sandgren, M., Paton, R. S., and Beckham, G. T. (2014) Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism. Proc. Natl. Acad. Sci. U.S.A. 111, 149-154
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. 149-154
    • Kim, S.1    Ståhlberg, J.2    Sandgren, M.3    Paton, R.S.4    Beckham, G.T.5
  • 50
    • 84908688781 scopus 로고    scopus 로고
    • Arapid quantitative activity assay shows that the Vibrio cholerae colonization factor GbpA is an active lytic polysaccharide monooxygenase
    • Loose, J. S., Forsberg, Z., Fraaije, M. W., Eijsink, V. G., and Vaaje-Kolstad, G. (2014)Arapid quantitative activity assay shows that the Vibrio cholerae colonization factor GbpA is an active lytic polysaccharide monooxygenase. FEBS Lett. 588, 3435-3440
    • (2014) FEBS Lett , vol.588 , pp. 3435-3440
    • Loose, J.S.1    Forsberg, Z.2    Fraaije, M.W.3    Eijsink, V.G.4    Vaaje-Kolstad, G.5
  • 51
    • 84877736930 scopus 로고    scopus 로고
    • Binding specificity and thermodynamics of cellulose-binding modules from Trichoderma reesei Cel7A and Cel6A
    • Guo, J., and Catchmark, J. M. (2013) Binding specificity and thermodynamics of cellulose-binding modules from Trichoderma reesei Cel7A and Cel6A. Biomacromolecules 14, 1268-1277
    • (2013) Biomacromolecules , vol.14 , pp. 1268-1277
    • Guo, J.1    Catchmark, J.M.2
  • 54
    • 84862173322 scopus 로고    scopus 로고
    • Production and effect of aldonic acids during enzymatic hydrolysis of lignocellulose at high dry matter content
    • Cannella, D., Hsieh, C. W., Felby, C., and Jørgensen, H. (2012) Production and effect of aldonic acids during enzymatic hydrolysis of lignocellulose at high dry matter content. Biotechnol. Biofuels 5, 26
    • (2012) Biotechnol. Biofuels , vol.5 , pp. 26
    • Cannella, D.1    Hsieh, C.W.2    Felby, C.3    Jørgensen, H.4
  • 55
    • 84930227196 scopus 로고    scopus 로고
    • Effects of lytic polysaccharide monooxygenase oxidation on cellulose structure and binding of oxidized cellulose oligomers to cellulases
    • Vermaas, J. V., Crowley, M. F., Beckham, G. T., and Payne, C. M. (2015) Effects of lytic polysaccharide monooxygenase oxidation on cellulose structure and binding of oxidized cellulose oligomers to cellulases. J. Phys. Chem. B 119, 6129-6143
    • (2015) J. Phys. Chem. B , vol.119 , pp. 6129-6143
    • Vermaas, J.V.1    Crowley, M.F.2    Beckham, G.T.3    Payne, C.M.4
  • 56
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


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