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Volumn 339, Issue 2, 2004, Pages 437-445

Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine

Author keywords

A. fumigatus phytase; covalent reaction intermediate; crystal structure; heat resistant; protein engineering; R.M.S., root mean square

Indexed keywords

ACID PHOSPHATASE; FUNGAL ENZYME; HISTIDINE; PHYTASE;

EID: 2342501800     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.03.057     Document Type: Article
Times cited : (58)

References (31)
  • 1
    • 0020331699 scopus 로고
    • Human prostatic acid phosphatase: A histidine phosphatase
    • van Etten R.L. Human prostatic acid phosphatase: a histidine phosphatase. Ann. NY Acad. Sci. 390:1982;27-51
    • (1982) Ann. NY Acad. Sci. , vol.390 , pp. 27-51
    • Van Etten, R.L.1
  • 2
    • 0026446318 scopus 로고
    • Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase
    • Ostanin K., Harms E.H., Stevis P.E., Kuciel R., Zhou M.M., van Etten R.L. Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase. J. Biol. Chem. 267:1992;22830-22836
    • (1992) J. Biol. Chem. , vol.267 , pp. 22830-22836
    • Ostanin, K.1    Harms, E.H.2    Stevis, P.E.3    Kuciel, R.4    Zhou, M.M.5    Van Etten, R.L.6
  • 3
    • 0033952704 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli phytase and its complex with phytate
    • Lim D., Golovan S., Forsberg C.W., Jia Z. Crystal structures of Escherichia coli phytase and its complex with phytate. Nature Struct. Biol. 7:2000;108-113
    • (2000) Nature Struct. Biol. , vol.7 , pp. 108-113
    • Lim, D.1    Golovan, S.2    Forsberg, C.W.3    Jia, Z.4
  • 4
    • 0029053544 scopus 로고
    • Phytate: A good or a bad food component
    • Harland B.F., Morris E.R. Phytate: a good or a bad food component. Nutr. Res. 15:1995;733-754
    • (1995) Nutr. Res. , vol.15 , pp. 733-754
    • Harland, B.F.1    Morris, E.R.2
  • 5
    • 0034304771 scopus 로고    scopus 로고
    • Nonphytate phosphorus requirement and phosphorus excretion of broiler chicks fed diets composed of normal or high available phosphate corn with and without microbial phytase
    • Waldroup P.W., Kersey J.H., Saleh E.A., Fritts C.A., Yan F., Stilborn H.L., et al. Nonphytate phosphorus requirement and phosphorus excretion of broiler chicks fed diets composed of normal or high available phosphate corn with and without microbial phytase. Poult. Sci. 10:2000;1451-1459
    • (2000) Poult. Sci. , vol.10 , pp. 1451-1459
    • Waldroup, P.W.1    Kersey, J.H.2    Saleh, E.A.3    Fritts, C.A.4    Yan, F.5    Stilborn, H.L.6
  • 6
    • 0031734945 scopus 로고    scopus 로고
    • Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase A. niger phytase, and A. niger PH 2.5 acid phosphatase
    • Wyss M., Pasamontes L., Remy R., Kohler J., Kusznir E., Gadient M., et al. Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase A. niger phytase, and A. niger PH 2.5 acid phosphatase. Appl. Environ. Microbiol. 64:1998;4446-4451
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4446-4451
    • Wyss, M.1    Pasamontes, L.2    Remy, R.3    Kohler, J.4    Kusznir, E.5    Gadient, M.6
  • 7
    • 0030898612 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus
    • Pasamontes L., Haiker M., Wyss M., Tessier M., van Loon A.P.G.M. Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus. Appl. Environ. Microbiol. 63:1997;1696-1700
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1696-1700
    • Pasamontes, L.1    Haiker, M.2    Wyss, M.3    Tessier, M.4    Van Loon, A.P.G.M.5
  • 8
    • 0033854732 scopus 로고    scopus 로고
    • Optimization of the catalytic properties of Aspergillus fumigatus phytase based on the three-dimensional structure
    • Tomschy A., Tessier M., Wyss M., Brugger R., Broger C., Schnoebelen L., et al. Optimization of the catalytic properties of Aspergillus fumigatus phytase based on the three-dimensional structure. Protein Sci. 9:2000;1304-1311
    • (2000) Protein Sci. , vol.9 , pp. 1304-1311
    • Tomschy, A.1    Tessier, M.2    Wyss, M.3    Brugger, R.4    Broger, C.5    Schnoebelen, L.6
  • 10
    • 0033591464 scopus 로고    scopus 로고
    • Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 24 Å resolution
    • Kostrewa D., Wyss M., D'Arcy A., van Loon A.P.G.M. Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 24 Å resolution. J. Mol. Biol. 288:1999;965-974
    • (1999) J. Mol. Biol. , vol.288 , pp. 965-974
    • Kostrewa, D.1    Wyss, M.2    D'Arcy, A.3    Van Loon, A.P.G.M.4
  • 11
    • 0024362443 scopus 로고
    • Carbohydrate removal fails to eliminate the heterogeneity of human prostatic acid phosphatase
    • Morris M.F., Waheed A., Risley J.M., van Etten R.L. Carbohydrate removal fails to eliminate the heterogeneity of human prostatic acid phosphatase. Clin. Chim. Acta. 182:1989;9-20
    • (1989) Clin. Chim. Acta , vol.182 , pp. 9-20
    • Morris, M.F.1    Waheed, A.2    Risley, J.M.3    Van Etten, R.L.4
  • 12
    • 0032146249 scopus 로고    scopus 로고
    • Comparison of glycosylation patterns of phytase from Aspergillus niger (A. ficuum) NRRL 3135 and recombinant phytase
    • Panchal T., Wodzinski R.J. Comparison of glycosylation patterns of phytase from Aspergillus niger (A. ficuum) NRRL 3135 and recombinant phytase. Prep. Biochem. Biotechnol. 28:1998;201-217
    • (1998) Prep. Biochem. Biotechnol. , vol.28 , pp. 201-217
    • Panchal, T.1    Wodzinski, R.J.2
  • 13
    • 0034673345 scopus 로고    scopus 로고
    • Expression of Aspergillus fumigatus phytase gene in Pichia pastoris and characterization of the recombinant enzyme
    • Rodriguez E., Mullaney E.J., Lei X.G. Expression of Aspergillus fumigatus phytase gene in Pichia pastoris and characterization of the recombinant enzyme. Biochem. Biophys. Res. Commun. 268:2000;373-378
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 373-378
    • Rodriguez, E.1    Mullaney, E.J.2    Lei, X.G.3
  • 14
    • 0035793607 scopus 로고    scopus 로고
    • High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase
    • Bond C.S., White M.F., Hunter W.N. High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase. J. Biol. Chem. 276:2001;3247-3253
    • (2001) J. Biol. Chem. , vol.276 , pp. 3247-3253
    • Bond, C.S.1    White, M.F.2    Hunter, W.N.3
  • 15
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt G., Woell S., Argos P. Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 269:1997;631-643
    • (1997) J. Mol. Biol. , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 16
    • 0032929094 scopus 로고    scopus 로고
    • Structural and mutagenesis studies of leishmania triosephosphate isomerase: A point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power
    • Williams J.C., Zeelen J.P., Neubauer G., Vriend G., Backmann J., Michels P.A., et al. Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power. Protein Eng. 12:1999;243-250
    • (1999) Protein Eng. , vol.12 , pp. 243-250
    • Williams, J.C.1    Zeelen, J.P.2    Neubauer, G.3    Vriend, G.4    Backmann, J.5    Michels, P.A.6
  • 17
    • 0036482260 scopus 로고    scopus 로고
    • The thermostability of DNA-binding protein HU from mesophilic, thermophilic, and extreme thermophilic bacteria
    • Christodoulou E., Vorgias C.E. The thermostability of DNA-binding protein HU from mesophilic, thermophilic, and extreme thermophilic bacteria. Extremophiles. 6:2002;21-31
    • (2002) Extremophiles , vol.6 , pp. 21-31
    • Christodoulou, E.1    Vorgias, C.E.2
  • 18
    • 0030062459 scopus 로고    scopus 로고
    • Amino-acid substitutions in a surface turn modulate protein stability
    • Predki P.F., Agrawal V., Brunger A.T., Regan L. Amino-acid substitutions in a surface turn modulate protein stability. Nature Struct. Biol. 3:1996;54-58
    • (1996) Nature Struct. Biol. , vol.3 , pp. 54-58
    • Predki, P.F.1    Agrawal, V.2    Brunger, A.T.3    Regan, L.4
  • 19
    • 0035830685 scopus 로고    scopus 로고
    • Thermostabilization of a chimeric enzyme by residue substitutions: Four amino acid residues in loop regions are responsible for the thermostability of Thermus thermophilus isopropylmalate dehydrogenase
    • Numata K., Hayashi-Iwasaki Y., Kawaguchi J., Sakurai M., Moriyama H., Tanaka N., Oshima T. Thermostabilization of a chimeric enzyme by residue substitutions: four amino acid residues in loop regions are responsible for the thermostability of Thermus thermophilus isopropylmalate dehydrogenase. Biochim. Biophys. Acta. 1545:2001;174-183
    • (2001) Biochim. Biophys. Acta , vol.1545 , pp. 174-183
    • Numata, K.1    Hayashi-Iwasaki, Y.2    Kawaguchi, J.3    Sakurai, M.4    Moriyama, H.5    Tanaka, N.6    Oshima, T.7
  • 20
    • 0031853167 scopus 로고    scopus 로고
    • Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain
    • Grantcharova V.P., Riddle D.S., Santiago J.V., Baker D. Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain. Nature Struct. Biol. 5:1998;714-720
    • (1998) Nature Struct. Biol. , vol.5 , pp. 714-720
    • Grantcharova, V.P.1    Riddle, D.S.2    Santiago, J.V.3    Baker, D.4
  • 21
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 23
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D, 50, 760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 24
    • 0030852350 scopus 로고    scopus 로고
    • Automated refinement for protein crystallography
    • Lamzin V.S., Wilson K.S. Automated refinement for protein crystallography. Methods Enzymol. 277:1997;269-305
    • (1997) Methods Enzymol. , vol.277 , pp. 269-305
    • Lamzin, V.S.1    Wilson, K.S.2
  • 25
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.K., Kjeldgaard M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta. Crystallog. sect. A. 47:1991;110-119
    • (1991) Acta. Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.K.3    Kjeldgaard, M.4
  • 26
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D. 53:1997;240-255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 27
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of molscript that include generally enhanced colouring capabilities
    • Esnouf R.M. An extensively modified version of molscript that include generally enhanced colouring capabilities. J. Mol. Graph Model. 15:1997;112-133
    • (1997) J. Mol. Graph Model , vol.15 , pp. 112-133
    • Esnouf, R.M.1
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 29
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 18:1997;2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


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