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Volumn 5, Issue 4, 1997, Pages 533-544

The crystal structure of rhamnogalacturonase a from Aspergillus aculeatus: A right-handed parallel β helix

Author keywords

glycosylation; hydrophobic cavity; rhamnogalacturonase A; right handed parallel helix

Indexed keywords

ASPERGILLUS ACULEATUS;

EID: 0031569829     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00209-8     Document Type: Article
Times cited : (130)

References (44)
  • 1
    • 0028533920 scopus 로고
    • Isolation and structural characterization of encto-rhamnogalacturonasegenerated fragments of the backbone of rhamnogalacturonan I
    • An, J., Zhang, L., O'Neill, M.A., Albersheim, P. & Darvill, A.G. (1994). Isolation and structural characterization of encto-rhamnogalacturonasegenerated fragments of the backbone of rhamnogalacturonan I. Carbohydr. Res. 264, 83-96.
    • (1994) Carbohydr. Res. , vol.264 , pp. 83-96
    • An, J.1    Zhang, L.2    O'Neill, M.A.3    Albersheim, P.4    Darvill, A.G.5
  • 2
    • 0000497441 scopus 로고
    • Structural features of hairy regions of pectins isolated from apple juice produced by the liquefraction process
    • Schols, H.A., Posthumus, M.A. & Voragen, A.G.J. (1990). Structural features of hairy regions of pectins isolated from apple juice produced by the liquefraction process. Carbohydr. Res. 206, 117-129.
    • (1990) Carbohydr. Res. , vol.206 , pp. 117-129
    • Schols, H.A.1    Posthumus, M.A.2    Voragen, A.G.J.3
  • 3
    • 0028143066 scopus 로고
    • Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus
    • Kofod, L.V., et al., & Dalbøge, H. (1994). Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus. J. Biol. Chem. 269, 29182-29189.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29182-29189
    • Kofod, L.V.1    Dalbøge, H.2
  • 4
    • 0030063641 scopus 로고    scopus 로고
    • Rhamnogalacturonase B from Aspergillus aculeatus is a rhamnogalacturonan α-L-rhamnopyranosyl-(1-4)- α-D-galactopyranosyluronide lyase
    • Mutter, M., Colquhoun, I.J., Schols, H.A., Beldman, G. & Voragen, A.G. (1996). Rhamnogalacturonase B from Aspergillus aculeatus is a rhamnogalacturonan α-L-rhamnopyranosyl-(1-4)- α-D-galactopyranosyluronide lyase. Plant Physiol. 110, 73-79.
    • (1996) Plant Physiol. , vol.110 , pp. 73-79
    • Mutter, M.1    Colquhoun, I.J.2    Schols, H.A.3    Beldman, G.4    Voragen, A.G.5
  • 5
    • 0028787502 scopus 로고
    • Molecular cloning and characterization of a rhamnogalacturonan acetylesterase from Aspergillus aculeatus: Synergism between rhamnogalacturonan degrading enzymes
    • Kauppinen, S., Christgau, S., Kofod, L.V., Halkier, T., Dörreich, K. & Dalbøge, H. (1995). Molecular cloning and characterization of a rhamnogalacturonan acetylesterase from Aspergillus aculeatus: synergism between rhamnogalacturonan degrading enzymes. J. Biol. Chem. 270, 27172-27178.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27172-27178
    • Kauppinen, S.1    Christgau, S.2    Kofod, L.V.3    Halkier, T.4    Dörreich, K.5    Dalbøge, H.6
  • 7
    • 0000129074 scopus 로고
    • The pectic polysaccharides of primary cell walls
    • Dey, P.M., ed. Academic press limited, London, UK
    • O'Neill, M., Albertsheim, P. & Darvill, A. (1990). The pectic polysaccharides of primary cell walls. In Methods in Plant Biochemistry. (Dey, P.M., ed.), pp. 415-441, Academic press limited, London, UK.
    • (1990) Methods in Plant Biochemistry , pp. 415-441
    • O'Neill, M.1    Albertsheim, P.2    Darvill, A.3
  • 8
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth
    • Carpita, N.C. & Gibeaut, D.M. (1993). Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. Plant J. 3, 1-30.
    • (1993) Plant J. , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 9
    • 0028393187 scopus 로고
    • Occurrence of pectic hairy regions in various plant cell wall materials and their degradability by rhamnogalacturonase
    • Schols, H.A. & Voragen, A.G.J. (1994). Occurrence of pectic hairy regions in various plant cell wall materials and their degradability by rhamnogalacturonase. Carbohydr. Res. 256, 83-95.
    • (1994) Carbohydr. Res. , vol.256 , pp. 83-95
    • Schols, H.A.1    Voragen, A.G.J.2
  • 10
    • 0344123202 scopus 로고
    • Characterisation of RG degradation products of new RGases using RG-rhamnohydrolase and RG-galacturonhydrolase
    • Visser J. & Voragen A.G.J., eds Elsvier Science B.V., Amsterdam, Netherlands
    • Mutter, M., Renard, C.M.G.C., Beldman, G., Schols, H.A. & Voragen A.G.J. (1995). Characterisation of RG degradation products of new RGases using RG-rhamnohydrolase and RG-galacturonhydrolase. In Proceedings of an International Symposium in Pectins and Pectinases. (Visser J. & Voragen A.G.J., eds), pp. 263-274, Elsvier Science B.V., Amsterdam, Netherlands.
    • (1995) Proceedings of An International Symposium in Pectins and Pectinases , pp. 263-274
    • Mutter, M.1    Renard, C.M.G.C.2    Beldman, G.3    Schols, H.A.4    Voragen, A.G.J.5
  • 14
    • 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
  • 15
    • 0027283042 scopus 로고
    • The parallel β helix of pectate lyase C: Something to sneeze at
    • Cohen, F.E. (1993). The parallel β helix of pectate lyase C: something to sneeze at. Science 260, 1444-1445.
    • (1993) Science , vol.260 , pp. 1444-1445
    • Cohen, F.E.1
  • 16
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt, G.J. & Jones, T.A. (1994). Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Cryst. D 50, 178-185.
    • (1994) Acta Cryst. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 17
    • 0028274954 scopus 로고
    • Intramolecular cavities in globular proteins
    • Hubbard, S.J., Gross, K.H. & Argos, P. (1994). Intramolecular cavities in globular proteins. Protein Eng. 7, 613-626.
    • (1994) Protein Eng. , vol.7 , pp. 613-626
    • Hubbard, S.J.1    Gross, K.H.2    Argos, P.3
  • 18
    • 0028607523 scopus 로고
    • Cavities and packing at protein interfaces
    • Hubbard, S.J. & Argos, P. (1994). Cavities and packing at protein interfaces. Protein Sci. 3, 2194-2206.
    • (1994) Protein Sci. , vol.3 , pp. 2194-2206
    • Hubbard, S.J.1    Argos, P.2
  • 19
    • 0028191528 scopus 로고    scopus 로고
    • The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwina chrysanthemi
    • Lietzke, S.E., Yoder, M.D., Keen, N.T. & Jurnak F. The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwina chrysanthemi. Plant Physiol. 106, 849-862.
    • Plant Physiol. , vol.106 , pp. 849-862
    • Lietzke, S.E.1    Yoder, M.D.2    Keen, N.T.3    Jurnak, F.4
  • 21
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertusis virulence factor P.69 pertactin
    • Emsley, P., Charles, I.G., Fairweather, N.F. & Isaacs, N.W. (1996). Structure of Bordetella pertusis virulence factor P.69 pertactin. Nature 381, 90-92.
    • (1996) Nature , vol.381 , pp. 90-92
    • Emsley, P.1    Charles, I.G.2    Fairweather, N.F.3    Isaacs, N.W.4
  • 22
    • 0028095571 scopus 로고
    • Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer
    • Steinbacher, S., Seckler, R., Miller, S., Steipe, B., Huber, R. & Reinemer, P. (1994). Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. Science 265, 383-386.
    • (1994) Science , vol.265 , pp. 383-386
    • Steinbacher, S.1    Seckler, R.2    Miller, S.3    Steipe, B.4    Huber, R.5    Reinemer, P.6
  • 23
    • 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
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and location of the errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard M. (1991). Improved methods for building protein models in electron-density maps and location of the errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies, G. & Henrissat, B. (1995). Structures and mechanisms of glycosyl hydrolases. Structure 3, 853-859.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 27
    • 0029916085 scopus 로고    scopus 로고
    • Inversion of configuration during hydrolysis of α-1,4-galacturonidic linkage by three Aspergillus polygalacturonases
    • Biely, P., Benen, J., Heinrichova, K., Kester, H.C.M. & Visser, J. (1996). Inversion of configuration during hydrolysis of α-1,4-galacturonidic linkage by three Aspergillus polygalacturonases. FEBS Lett. 382, 249-255.
    • (1996) FEBS Lett. , vol.382 , pp. 249-255
    • Biely, P.1    Benen, J.2    Heinrichova, K.3    Kester, H.C.M.4    Visser, J.5
  • 28
    • 0031005266 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray studies of recombinant rhamnogalacturonase A from Aspergillus aculeatus
    • Petersen, T.N., Christgau, S., Kofod, L.V., Kauppinen, S., Dalbøge H. & Larsen S. (1997). Crystallization and preliminary X-ray studies of recombinant rhamnogalacturonase A from Aspergillus aculeatus. Acta Cryst. D 53, 105-107.
    • (1997) Acta Cryst. D , vol.53 , pp. 105-107
    • Petersen, T.N.1    Christgau, S.2    Kofod, L.V.3    Kauppinen, S.4    Dalbøge, H.5    Larsen, S.6
  • 29
    • 0028341842 scopus 로고
    • Refined crystal structure of glucoamylase from Aspergillus awamori var. X100
    • Aleshin, A.E., Hoffman, C., Firsov, L.M. & Honzatko, R.B. (1994). Refined crystal structure of glucoamylase from Aspergillus awamori var. X100. J. Mol. Biol. 238, 575-591.
    • (1994) J. Mol. Biol. , vol.238 , pp. 575-591
    • Aleshin, A.E.1    Hoffman, C.2    Firsov, L.M.3    Honzatko, R.B.4
  • 30
    • 0017684280 scopus 로고
    • Structure of a carbohydrate moiety of a unit A glycopeptide of calf thyroglobulin
    • Ito S., Yamashita K., Spiro, R.G. & Kobata, A. (1977). Structure of a carbohydrate moiety of a unit A glycopeptide of calf thyroglobulin. J. Biochem. 81, 1621-1629.
    • (1977) J. Biochem. , vol.81 , pp. 1621-1629
    • Ito, S.1    Yamashita, K.2    Spiro, R.G.3    Kobata, A.4
  • 31
    • 0542368163 scopus 로고
    • Pectic enzymes
    • Blanshard, J.M.V. & Mitchell, J.R., eds, Butterworths, London
    • Pilnik, W. & Rombouts, F.M. (1979). Pectic enzymes. In Polysaccharides in Food. (Blanshard, J.M.V. & Mitchell, J.R., eds), pp. 109-126, Butterworths, London.
    • (1979) Polysaccharides in Food , pp. 109-126
    • Pilnik, W.1    Rombouts, F.M.2
  • 32
    • 0024619692 scopus 로고
    • Production of cell wall degrading enzymes by aspergillus nidulans: A model system for fungal pathogenesis of plants
    • Dean, R.A. & Timberlake, W.E. (1989). Production of cell wall degrading enzymes by aspergillus nidulans: a model system for fungal pathogenesis of plants. Plant Cell 1, 265-273.
    • (1989) Plant Cell , vol.1 , pp. 265-273
    • Dean, R.A.1    Timberlake, W.E.2
  • 33
    • 0024619547 scopus 로고
    • Regulation of the Aspergillus nidulans pectate lyase gene
    • Dean, R.A. & Timberlake, W.E. (1989). Regulation of the Aspergillus nidulans pectate lyase gene. Plant Cell 1, 275-284.
    • (1989) Plant Cell , vol.1 , pp. 275-284
    • Dean, R.A.1    Timberlake, W.E.2
  • 34
    • 0025105710 scopus 로고
    • Cloning and expression of a second aspergillus niger pectin lyase gene (pelA): Indications of a pectin lyase gene family in A. niger
    • Harmsen, J.A.M., Kusters-van Someren, M.A. & Visser, J. (1990). Cloning and expression of a second aspergillus niger pectin lyase gene (pelA): indications of a pectin lyase gene family in A. niger. Curr. Genet. 18, 161-166.
    • (1990) Curr. Genet. , vol.18 , pp. 161-166
    • Harmsen, J.A.M.1    Kusters-van Someren, M.A.2    Visser, J.3
  • 35
    • 0025776007 scopus 로고
    • Pectinase production by Neurospora crassa: Purification and biochemical characterization of extracellular polygalacturonase activity
    • Polizeli, M.LT.M., Jorge, J.A. & Terenzi, H.F. (1991). Pectinase production by Neurospora crassa: purification and biochemical characterization of extracellular polygalacturonase activity. J. Gen. Microbiol. 137, 1815-1823.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 1815-1823
    • Polizeli, M.L.T.M.1    Jorge, J.A.2    Terenzi, H.F.3
  • 36
    • 0026646374 scopus 로고
    • The polygalacturonases of Aspergillus niger are encoded by a family of diverged genes
    • Bussink., H.J.D., Buxton, F.P., Fraaye, B.A., de Graaf, L.H. & Visser, J. (1992). The polygalacturonases of Aspergillus niger are encoded by a family of diverged genes. Eur. J. Biochem. 208, 83-90.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 83-90
    • Bussink, H.J.D.1    Buxton, F.P.2    Fraaye, B.A.3    De Graaf, L.H.4    Visser, J.5
  • 38
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No.4
    • Collaborative Computational Project No.4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 40
    • 0030498233 scopus 로고    scopus 로고
    • xdlMAPMAN and xdlDATAMAN: Programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection datasets
    • Kleywegt, G.J. & Jones, T.A. (1996). xdlMAPMAN and xdlDATAMAN: programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection datasets. Acta Cryst. D 52, 826-828.
    • (1996) Acta Cryst. D , vol.52 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 41
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, AT. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 42
    • 0000243829 scopus 로고
    • PROCHECK: A program to check, the stereochemical quality of a protein structure
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check, the stereochemical quality of a protein structure. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 43
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • Kabsch, W. & 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
  • 44
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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