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Volumn 5, Issue 5, 1997, Pages 677-689

Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases

Author keywords

crystal structure; parallel helix; pectin lyase; pH conformational change; substrate specificity

Indexed keywords


EID: 0031570284     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00222-0     Document Type: Article
Times cited : (181)

References (36)
  • 1
    • 0002508652 scopus 로고
    • Pectic enzymes
    • (Birch, G.G., Blakebrough, N. & Parker, K.J., eds), Applied Science Publishers Ltd., London, UK
    • Pilnik, W. & Rombouts, P.M. (1981). Pectic enzymes. In Enzymes and Food Processing. (Birch, G.G., Blakebrough, N. & Parker, K.J., eds), pp. 105-128, Applied Science Publishers Ltd., London, UK.
    • (1981) Enzymes and Food Processing , pp. 105-128
    • Pilnik, W.1    Rombouts, P.M.2
  • 2
    • 0025220288 scopus 로고
    • Molecular and genetic characterization of two pollen-expressed genes that have sequence similarity to pectate lyases of the plant pathogen Erwinia
    • Wing, R.A., Yamaguchi, J., Larabell, S.K., Ursin, V.M. & McCormick, S. (1989). Molecular and genetic characterization of two pollen-expressed genes that have sequence similarity to pectate lyases of the plant pathogen Erwinia. Plant Mol. Biol. 14, 17-28.
    • (1989) Plant Mol. Biol. , vol.14 , pp. 17-28
    • Wing, R.A.1    Yamaguchi, J.2    Larabell, S.K.3    Ursin, V.M.4    McCormick, S.5
  • 4
    • 0000980748 scopus 로고
    • The role of pectic enzymes in plant pathogenesis
    • Collmer, A. & Keen, N.T. (1986). The role of pectic enzymes in plant pathogenesis. Annu. Rev. Phytopathol. 24, 383-409.
    • (1986) Annu. Rev. Phytopathol. , vol.24 , pp. 383-409
    • Collmer, A.1    Keen, N.T.2
  • 6
    • 0025206677 scopus 로고
    • New and future uses of enzymes in food processing
    • Whitaker, J.R. (1990). New and future uses of enzymes in food processing. Food Biotechnol. 4, 669-697.
    • (1990) Food Biotechnol. , vol.4 , pp. 669-697
    • Whitaker, J.R.1
  • 7
    • 0029257437 scopus 로고
    • Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily
    • Henrissat, B., Heffron, S.E., Yoder, M.D., Lietzke, S.E. & Jurnak, F. (1995). Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily. Plant Physiol. 107, 963-976.
    • (1995) Plant Physiol. , vol.107 , pp. 963-976
    • Henrissat, B.1    Heffron, S.E.2    Yoder, M.D.3    Lietzke, S.E.4    Jurnak, F.5
  • 8
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C, a secreted plant virulence factor
    • Yoder, M.D., Keen, N.T. & Jurnak, F. (1993). New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science 260, 1503-1507.
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 9
    • 0028191528 scopus 로고
    • The three-dimensional structure of pectate lyase E, a plant virulence factor from E. chrysanthemi
    • Lietzke, S.E., Yoder, M.D., Keen, N.T. & Jurnak, F. (1994). The three-dimensional structure of pectate lyase E, a plant virulence factor from E. chrysanthemi. Plant Physiol. 106, 849-862.
    • (1994) Plant Physiol. , vol.106 , pp. 849-862
    • Lietzke, S.E.1    Yoder, M.D.2    Keen, N.T.3    Jurnak, F.4
  • 11
    • 0023434016 scopus 로고
    • Pectate lyase from Fusarium solani f sp. pisi: Purification, characterization, in vitro translation of the mRNA, and involvement in pathogenicity
    • Crawford, M. & Kolattukudy, P.E. (1987). Pectate lyase from Fusarium solani f sp. pisi: purification, characterization, in vitro translation of the mRNA, and involvement in pathogenicity. Arch. Biochem. Biophys. 258, 196-205.
    • (1987) Arch. Biochem. Biophys. , vol.258 , pp. 196-205
    • Crawford, M.1    Kolattukudy, P.E.2
  • 12
    • 0029861087 scopus 로고    scopus 로고
    • Differential effect of site-directed mutations in PelC on pectate lyase activity, plant-tissue maceration, and elicitor activity
    • Kita, N., Boyd, C.M., Garrett, M.R., Jurnak, F. & Keen, N.T. (1996). Differential effect of site-directed mutations in PelC on pectate lyase activity, plant-tissue maceration, and elicitor activity. J. Biol. Chem. 43, 26529-26535.
    • (1996) J. Biol. Chem. , vol.43 , pp. 26529-26535
    • Kita, N.1    Boyd, C.M.2    Garrett, M.R.3    Jurnak, F.4    Keen, N.T.5
  • 13
    • 0004191979 scopus 로고
    • PhD thesis. Agricultural University, Wageningen, The Netherlands
    • Van Houdenhoven, F.E.A. (1975). Studies on pectin lyase. PhD thesis. Agricultural University, Wageningen, The Netherlands.
    • (1975) Studies on Pectin Lyase
    • Van Houdenhoven, F.E.A.1
  • 15
    • 0028174858 scopus 로고
    • Functional and structural role of a tryptophan generally observed in protein-carbohydrate interaction
    • Maenaka, K., Kawai, G., Watanabe, K., Sunada, F. & Kumagai, I. (1994). Functional and structural role of a tryptophan generally observed in protein-carbohydrate interaction. J. Biol. Chem. 269, 7070-7075.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7070-7075
    • Maenaka, K.1    Kawai, G.2    Watanabe, K.3    Sunada, F.4    Kumagai, I.5
  • 16
    • 0026319774 scopus 로고
    • Recognition of a cellsurface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment
    • Cygler, M., Rose, D.R. & Bundle, D.R. (1991). Recognition of a cellsurface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment. Science 253, 442-445.
    • (1991) Science , vol.253 , pp. 442-445
    • Cygler, M.1    Rose, D.R.2    Bundle, D.R.3
  • 17
    • 0025910182 scopus 로고
    • Structure of the Aspergillus niger pelA gene and its expression in Aspergillus niger and Aspergillus nidulans
    • Kusters-van Someren, M.A., Harmsen, J.A.M., Kester, H.C.M. & Visser, J. (1991). Structure of the Aspergillus niger pelA gene and its expression in Aspergillus niger and Aspergillus nidulans. Curr. Genet. 20, 293-299.
    • (1991) Curr. Genet. , vol.20 , pp. 293-299
    • Kusters-van Someren, M.A.1    Harmsen, J.A.M.2    Kester, H.C.M.3    Visser, J.4
  • 19
    • 0030063034 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of pectin lyase A from Aspergillus niger
    • Jenkins, J., et al., & Gravesen, T. (1996). Crystallization and preliminary X-ray analysis of pectin lyase A from Aspergillus niger. Acta Cryst. D 52, 402-404.
    • (1996) Acta Cryst. D , vol.52 , pp. 402-404
    • Jenkins, J.1    Gravesen, T.2
  • 20
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik, J. & Kim, S.H. (1991). Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Cryst. 24, 409-411.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.H.2
  • 21
    • 84920325457 scopus 로고
    • AMoRe - An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe - an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
    • (1994) Acta Cryst. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 22
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-767.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-767
  • 23
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy-atom parameters
    • (Wolf, W. & Leslie, A.G.W., eds), SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1991). Maximum likelihood refinement of heavy-atom parameters. In Isomorphous Replacement and Anomalous Scattering. (Wolf, W. & Leslie, A.G.W., eds), pp. 80-86, SERC Daresbury Laboratory, Warrington, UK.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 24
    • 0000771669 scopus 로고
    • Structure-factor probabilities for related structures
    • Read, R.J. (1990). Structure-factor probabilities for related structures. Acta Cryst. A 46, 900-912.
    • (1990) Acta Cryst. A , vol.46 , pp. 900-912
    • Read, R.J.1
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these maps
    • Jones, T.A., Zou, J.-T., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron-density maps and the location of errors in these maps. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-T.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 27
  • 29
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, AT., Kuriyan, J. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 30
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein-structure refinement
    • Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein-structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 31
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 32
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. & Wilson, K.S. (1993). Automated refinement of protein models. Acta Cryst. D 49, 129-147.
    • (1993) Acta Cryst. D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 33
    • 0026655361 scopus 로고
    • Stereochemical quality of protein structure coordinates
    • Morris, A.L., MacArthur, M.W. & Thornton, J.M. (1992). Stereochemical quality of protein structure coordinates. Proteins 12, 345-364.
    • (1992) Proteins , vol.12 , pp. 345-364
    • Morris, A.L.1    MacArthur, M.W.2    Thornton, J.M.3
  • 34
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of proteins
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of proteins. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 35
    • 0343889438 scopus 로고
    • Molecular Simulations Inc. 16, New England Executive Park., Burlington, MA, 01803-5297. USA
    • QUANTA 4.0. (1994). Molecular Simulations Inc. 16, New England Executive Park., Burlington, MA, 01803-5297. USA.
    • (1994) QUANTA 4.0
  • 36
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface-properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: graphical representation and analysis of surface-properties. Biophys. J. 64, 166.
    • (1993) Biophys. J. , vol.64 , pp. 166
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.