메뉴 건너뛰기




Volumn 20, Issue 6, 2012, Pages 1051-1061

Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC AMINO ACID; OXYGEN DERIVATIVE; POLYSACCHARIDE; POLYSACCHARIDE MONOOXYGENASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 84861987031     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.04.002     Document Type: Article
Times cited : (243)

References (46)
  • 3
    • 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
  • 5
    • 0037393779 scopus 로고    scopus 로고
    • Bond dissociation energies of organic molecules
    • Blanksby, S.J., and Ellison, G.B. (2003). Bond dissociation energies of organic molecules. Acc. Chem. Res. 36, 255-263.
    • (2003) Acc. Chem. Res. , vol.36 , pp. 255-263
    • Blanksby, S.J.1    Ellison, G.B.2
  • 6
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • Boraston, A.B., Bolam, D.N., Gilbert, H.J., and Davies, G.J. (2004). Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem. J. 382, 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
  • 7
    • 0034055545 scopus 로고    scopus 로고
    • Structural changes in a cryo-cooled protein crystal owing to radiation damage
    • Burmeister, W.P. (2000). Structural changes in a cryo-cooled protein crystal owing to radiation damage. Acta Crystallogr. D Biol. Crystallogr. 56, 328-341.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 328-341
    • Burmeister, W.P.1
  • 8
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): An expert resource for Glycogenomics
    • Cantarel, B.L., Coutinho, P.M., Rancurel, C., Bernard, T., Lombard, V., and Henrissat, B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 37 (Database issue), D233-D238.
    • (2009) Nucleic Acids Res. , vol.37 , Issue.DATABASE ISSUE
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5    Henrissat, B.6
  • 9
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: An initial-stage protein-docking algorithm
    • Chen, R., Li, L., and Weng, Z. (2003). ZDOCK: an initial-stage protein-docking algorithm. Proteins 52, 80-87.
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4.
    • Collaborative Computational Project, Number 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Section D 50, 760-763.
    • (1994) Acta Crystallogr. Section D , vol.50 , pp. 760-763
  • 12
  • 17
    • 80052188856 scopus 로고    scopus 로고
    • Improving the bioconversion of plant biomass to biofuels: A multidisciplinary approach
    • Galazka, J.M., and Cate, J.H.D. (2011). Improving the bioconversion of plant biomass to biofuels: A multidisciplinary approach. Energ. Environ. Sci. 4, 3329-3333.
    • (2011) Energ. Environ. Sci. , vol.4 , pp. 3329-3333
    • Galazka, J.M.1    Cate, J.H.D.2
  • 18
    • 0029895160 scopus 로고    scopus 로고
    • Electron transfer in proteins
    • Gray, H.B., and Winkler, J.R. (1996). Electron transfer in proteins. Annu. Rev. Biochem. 65, 537-561.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 537-561
    • Gray, H.B.1    Winkler, J.R.2
  • 19
    • 0034650750 scopus 로고    scopus 로고
    • A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase
    • Hallberg, B.M., Bergfors, T., Bäckbro, K., Pettersson, G., Henriksson, G., and Divne, C. (2000). A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase. Structure 8, 79-88.
    • (2000) Structure , vol.8 , pp. 79-88
    • Hallberg, B.M.1    Bergfors, T.2    Bäckbro, K.3    Pettersson, G.4    Henriksson, G.5    Divne, C.6
  • 20
    • 77950948151 scopus 로고    scopus 로고
    • Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: Structure and function of a large, enigmatic family
    • Harris, P.V., Welner, D., McFarland, K.C., Re, E., Navarro Poulsen, J.C., Brown, K., Salbo, R., Ding, H., Vlasenko, E., Merino, S., et al. (2010). Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: structure and function of a large, enigmatic family. Biochemistry 49, 3305-3316.
    • (2010) Biochemistry , vol.49 , pp. 3305-3316
    • Harris, P.V.1    Welner, D.2    McFarland, K.C.3    Re, E.4    Navarro Poulsen, J.C.5    Brown, K.6    Salbo, R.7    Ding, H.8    Vlasenko, E.9    Merino, S.10
  • 21
    • 0000588956 scopus 로고
    • Stability of polyatomic molecules in degenerate electronic states. I. Orbital degeneracy
    • Jahn, H.A., and Teller, E. (1937). Stability of polyatomic molecules in degenerate electronic states. I. Orbital degeneracy. Proc. R. Soc. Lon. Ser. A 161, 220-235.
    • (1937) Proc. R. Soc. Lon. Ser. A , vol.161 , pp. 220-235
    • Jahn, H.A.1    Teller, E.2
  • 22
    • 52049106382 scopus 로고    scopus 로고
    • The first structure of a glycoside hydrolase family 61 member, Cel61B from Hypocrea jecorina, at 1.6 A resolution
    • Karkehabadi, S., Hansson, H., Kim, S., Piens, K., Mitchinson, C., and Sandgren, M. (2008). The first structure of a glycoside hydrolase family 61 member, Cel61B from Hypocrea jecorina, at 1.6 A resolution. J. Mol. Biol. 383, 144-154.
    • (2008) J. Mol. Biol. , vol.383 , pp. 144-154
    • Karkehabadi, S.1    Hansson, H.2    Kim, S.3    Piens, K.4    Mitchinson, C.5    Sandgren, M.6
  • 23
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • Katoh, K., and Toh, H. (2008). Recent developments in the MAFFT multiple sequence alignment program. Brief. Bioinform. 9, 286-298.
    • (2008) Brief. Bioinform. , vol.9 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 24
    • 33645637817 scopus 로고    scopus 로고
    • The copper-enzyme family of dopamine beta-monooxygenase and peptidylglycine alpha-hydroxylating monooxygenase: Resolving the chemical pathway for substrate hydroxylation
    • Klinman, J.P. (2006). The copper-enzyme family of dopamine beta-monooxygenase and peptidylglycine alpha-hydroxylating monooxygenase: resolving the chemical pathway for substrate hydroxylation. J. Biol. Chem. 281, 3013-3016.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3013-3016
    • Klinman, J.P.1
  • 25
    • 0024962351 scopus 로고
    • Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
    • Kraulis, J., Clore, G.M., Nilges, M., Jones, T.A., Pettersson, G., Knowles, J., and Gronenborn, A.M. (1989). Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry 28, 7241-7257.
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 26
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E., and Henrick, K. (2004). Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60, 2256-2268.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 27
    • 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
  • 28
    • 0030860744 scopus 로고    scopus 로고
    • A CP/MAS C-13 NMR investigation of molecular ordering in celluloses
    • Larsson, P.T., Wickholm, K., and Iversen, T. (1997). A CP/MAS C-13 NMR investigation of molecular ordering in celluloses. Carbohydr. Res. 302, 19-25.
    • (1997) Carbohydr. Res. , vol.302 , pp. 19-25
    • Larsson, P.T.1    Wickholm, K.2    Iversen, T.3
  • 29
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy, D.J., Aukhil, I., and Erickson, H.P. (1996). 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84, 155-164.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 30
    • 0035073965 scopus 로고    scopus 로고
    • Atomic resolution structures of trypsin provide insight into structural radiation damage
    • Leiros, H.K.S., McSweeney, S.M., and Smalås, A.O. (2001). Atomic resolution structures of trypsin provide insight into structural radiation damage. Acta Crystallogr. D Biol. Crystallogr. 57, 488-497.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 488-497
    • Leiros, H.K.S.1    McSweeney, S.M.2    Smalås, A.O.3
  • 31
    • 33644870851 scopus 로고    scopus 로고
    • Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection?
    • Leiros, H.K.S., Timmins, J., Ravelli, R.B.G., and McSweeney, S.M. (2006). Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection? Acta Crystallogr. D Biol. Crystallogr. 62, 125-132.
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 125-132
    • Leiros, H.K.S.1    Timmins, J.2    Ravelli, R.B.G.3    McSweeney, S.M.4
  • 34
    • 0037036704 scopus 로고    scopus 로고
    • Crystal structure and hydrogen-bonding system in cellulose Ibeta from synchrotron X-ray and neutron fiber diffraction
    • Nishiyama, Y., Langan, P., and Chanzy, H. (2002). Crystal structure and hydrogen-bonding system in cellulose Ibeta from synchrotron X-ray and neutron fiber diffraction. J. Am. Chem. Soc. 124, 9074-9082.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9074-9082
    • Nishiyama, Y.1    Langan, P.2    Chanzy, H.3
  • 35
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D.G., and Heringa, J. (2000). T-Coffee: A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205-217.
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 38
    • 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
  • 40
    • 0026706824 scopus 로고
    • Crystal structure of human immunoglobulin fragment Fab New refined at 2.0 A resolution
    • Saul, F.A., and Poljak, R.J. (1992). Crystal structure of human immunoglobulin fragment Fab New refined at 2.0 A resolution. Proteins 14, 363-371.
    • (1992) Proteins , vol.14 , pp. 363-371
    • Saul, F.A.1    Poljak, R.J.2
  • 44
    • 15744367514 scopus 로고    scopus 로고
    • Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21
    • Vaaje-Kolstad, G., Houston, D.R., Riemen, A.H., Eijsink, V.G., and van Aalten, D.M. (2005). Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21. J. Biol. Chem. 280, 11313-11319.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11313-11319
    • Vaaje-Kolstad, G.1    Houston, D.R.2    Riemen, A.H.3    Eijsink, V.G.4    Van Aalten, D.M.5
  • 45
    • 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
  • 46
    • 67649815010 scopus 로고    scopus 로고
    • Cellulases and biofuels
    • Wilson, D.B. (2009). Cellulases and biofuels. Curr. Opin. Biotechnol. 20, 295-299.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 295-299
    • Wilson, D.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.