메뉴 건너뛰기




Volumn 288, Issue 5, 1999, Pages 965-974

Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4 Å resolution

Author keywords

Acid phosphatase; Aspergillus niger; Crystal structure; Protein crystallography; Tetramer

Indexed keywords

ACID PHOSPHATASE;

EID: 0033591464     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2736     Document Type: Article
Times cited : (94)

References (39)
  • 2
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Bruenger A. T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Bruenger, A.T.1
  • 3
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Bruenger A. T., Kuriyan J., Karplus M. Crystallographic R factor refinement by molecular dynamics. Science. 235:1987;458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Bruenger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 5
    • 0027943884 scopus 로고
    • A structural analysis of phosphate and sulfate binding sites in proteins
    • Copley R. R., Barton G. J. A structural analysis of phosphate and sulfate binding sites in proteins. J. Mol. Biol. 242:1994;321-329.
    • (1994) J. Mol. Biol. , vol.242 , pp. 321-329
    • Copley, R.R.1    Barton, G.J.2
  • 6
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de la Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276:1997;472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 7
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R. A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A. 47:1991;392-400.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 8
    • 0029315603 scopus 로고
    • MAB: A generally applicable molecular force field for structure modelling in medicinal chemistry
    • Gerber P. R., Müller K. MAB: A generally applicable molecular force field for structure modelling in medicinal chemistry. J. Computer-Aided Mol. Design. 9:1995;251-268.
    • (1995) J. Computer-Aided Mol. Design , vol.9 , pp. 251-268
    • Gerber, P.R.1    Müller, K.2
  • 9
    • 0030451745 scopus 로고    scopus 로고
    • Deglycosylation of protein for crystallization using recombinant fusion protein glycosidases
    • Grueninger-Leitch F., D'Arcy A., D'Arcy B., Chène C. Deglycosylation of protein for crystallization using recombinant fusion protein glycosidases. Protein Sci. 5:1996;2617-2622.
    • (1996) Protein Sci. , vol.5 , pp. 2617-2622
    • Grueninger-Leitch, F.1    D'Arcy, A.2    D'Arcy, B.3    Chène, C.4
  • 11
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction
    • Jiang J.-S., Bruenger A. T. Protein hydration observed by X-ray diffraction. J. Mol. Biol. 243:1994;100-115.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.-S.1    Bruenger, A.T.2
  • 12
    • 0022701772 scopus 로고
    • Using known substructures in protein model building and crystallography
    • Jones T. A., Thirup S. Using known substructures in protein model building and crystallography. EMBO J. 5:1986;819-822.
    • (1986) EMBO J. , vol.5 , pp. 819-822
    • Jones, T.A.1    Thirup, S.2
  • 13
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch W. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallog. 21:1988;916-924.
    • (1988) J. Appl. Crystallog. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 14
    • 0002765199 scopus 로고    scopus 로고
    • Bulk solvent correction: Practical application and effects in real and reciprocal space
    • Kostrewa d. Bulk solvent correction: practical application and effects in real and reciprocal space. Jt. CCP4 ESF-EACBM Newslett. Protein Crystallog. 34:1997;9-22.
    • (1997) Jt. CCP4 ESF-EACBM Newslett. Protein Crystallog. , vol.34 , pp. 9-22
    • Kostrewa, D.1
  • 16
    • 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
  • 17
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 18
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.1
  • 19
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E. A., Bacon D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 20
    • 0031034203 scopus 로고    scopus 로고
    • The phytase subfamily of histidine acid phosphatases: Isolation of genes for two novel phytases from the fungiAspergillus terreus and Myceliophthora thermophila
    • Mitchell D. B., Vogel K., Weimann B. J., Pasamontes L., van Loon A. P. G. M. The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungiAspergillus terreus and Myceliophthora thermophila. Microbiology. 143:1997;245-252.
    • (1997) Microbiology , vol.143 , pp. 245-252
    • Mitchell, D.B.1    Vogel, K.2    Weimann, B.J.3    Pasamontes, L.4    Van Loon, A.P.G.M.5
  • 21
    • 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
    • 0027340545 scopus 로고
    • Asp304 of Escherichia coli acid phosphatase is involved in leaving group protonation
    • Ostanin K., van Etten R. L. Asp304 of Escherichia coli acid phosphatase is involved in leaving group protonation. J. Biol. Chem. 268:1993;20778-20784.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20778-20784
    • Ostanin, K.1    Van Etten, R.L.2
  • 24
    • 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
  • 27
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with error
    • Read R. J. Improved Fourier coefficients for maps using phases from partial structures with error. Acta Crystallog. sect. A. 42:1986;140-149.
    • (1986) Acta Crystallog. Sect. a , vol.42 , pp. 140-149
    • Read, R.J.1
  • 28
    • 0027201613 scopus 로고
    • Three-dimensional structure of rat acid phosphatase
    • Schneider G., Lindqvist Y., Vihko P. Three-dimensional structure of rat acid phosphatase. EMBO J. 12:1993;2609-2615.
    • (1993) EMBO J. , vol.12 , pp. 2609-2615
    • Schneider, G.1    Lindqvist, Y.2    Vihko, P.3
  • 29
    • 0002812783 scopus 로고
    • The application of direct methods and Patterson interpretation to high-resolution native protein data
    • Sheldrick G. M., Daunter Z., Wilson K. S., Hope H., Sieker L. C. The application of direct methods and Patterson interpretation to high-resolution native protein data. Acta Crystallog. sect. A. 49:1993;18-23.
    • (1993) Acta Crystallog. Sect. a , vol.49 , pp. 18-23
    • Sheldrick, G.M.1    Daunter, Z.2    Wilson, K.S.3    Hope, H.4    Sieker, L.C.5
  • 30
    • 0024237908 scopus 로고
    • Aspergillus ficuum phytase: Partial primary structure, substrate selectivity, and kinetic characterization
    • Ullah A. H. J. Aspergillus ficuum phytase: partial primary structure, substrate selectivity, and kinetic characterization. Prep. Biochem. 18:1988;459-471.
    • (1988) Prep. Biochem. , vol.18 , pp. 459-471
    • Ullah, A.H.J.1
  • 31
    • 0023493960 scopus 로고
    • Purification, N-terminal amino acid sequence and characterization of pH 2.5 optimum acid phosphatase (EC 3.1.3.2) from Aspergillus ficuum
    • Ullah A. H. J., Cummins B. J. Purification, N-terminal amino acid sequence and characterization of pH 2.5 optimum acid phosphatase (EC 3.1.3.2) from Aspergillus ficuum. Prep. Biochem. 17:1987;397-422.
    • (1987) Prep. Biochem. , vol.17 , pp. 397-422
    • Ullah, A.H.J.1    Cummins, B.J.2
  • 32
    • 0023080759 scopus 로고
    • Extracellular phytase (EC 3.1.3.8) from Aspergillus ficuum NRRL 3135: Purification and characterization
    • Ullah A. H. J., Gibson D. M. Extracellular phytase (EC 3.1.3.8) from Aspergillus ficuum NRRL 3135: purification and characterization. Prep. Biochem. 17:1987;63-91.
    • (1987) Prep. Biochem. , vol.17 , pp. 63-91
    • Ullah, A.H.J.1    Gibson, D.M.2
  • 33
    • 0000464339 scopus 로고
    • Substrate selectivity in Aspergillus ficuum phytase and acid phosphatase using myo -inositol phosphates
    • Ullah A. H. J., Phillippy B. Q. Substrate selectivity in Aspergillus ficuum phytase and acid phosphatase using myo -inositol phosphates. J. Agric. Food Chem. 42:1994;423-425.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 423-425
    • Ullah, A.H.J.1    Phillippy, B.Q.2
  • 34
    • 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
  • 35
    • 0345038822 scopus 로고    scopus 로고
    • A heat-resistance phytase of Aspergillus fumigatus with superior performance in animal experiments. Phytase optimization and natural variability
    • S. K. Rasmussen, V. Raboy, H. Dalbøge, & F. Loewus. Dordrecht,: Kluwer Academic Publishers
    • van Loon A. P. G. M., Simoes-Nunes C., Wyss M., Tomschy A., Vogel K., Pasamontes L. A heat-resistance phytase of Aspergillus fumigatus with superior performance in animal experiments. Phytase optimization and natural variability. Rasmussen S. K., Raboy V., Dalbøge H., Loewus F. The Biochemistry of Phytate and Phytases. 1999;Kluwer Academic Publishers, Dordrecht
    • (1999) The Biochemistry of Phytate and Phytases
    • Van Loon, A.P.G.M.1    Simoes-Nunes, C.2    Wyss, M.3    Tomschy, A.4    Vogel, K.5    Pasamontes, L.6
  • 36
    • 0026535321 scopus 로고
    • Hydrolysis of phosphate monoesters: A biological problem with multiple chemical solutions
    • Vincent J. B., Crowder M. W., Averill B. A. Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions. Trends Biochem. Sci. 17:1992;105-110.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 105-110
    • Vincent, J.B.1    Crowder, M.W.2    Averill, B.A.3
  • 39
    • 0004091818 scopus 로고
    • Oxford: Wm. C. Brown Publishers. p. 151-153
    • Zubay G. Biochemistry. 1993;Wm. C. Brown Publishers, Oxford. p. 151-153.
    • (1993) Biochemistry
    • Zubay, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.