메뉴 건너뛰기




Volumn 7, Issue 8, 1999, Pages 977-988

Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: An enzyme involved in the tyrosine degradation pathway

Author keywords

Crystal; Dioxygenase; Herbicide; Iron; Tyrosinemia

Indexed keywords

4 HYDROXYPHENYLPYRUVATE DIOXYGENASE; BACTERIAL ENZYME; CATECHOL 2,3 DIOXYGENASE; HOMOGENTISIC ACID; IRON; OXYGEN; PIGMENT; PYRUVIC ACID; QUINONE DERIVATIVE; TOCOPHEROL; TYROSINE;

EID: 0033566995     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80124-5     Document Type: Article
Times cited : (139)

References (50)
  • 1
    • 0020422576 scopus 로고
    • Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp strain P.J.874
    • Lindstedt, S. & Rundgren, M. (1982). Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp strain P.J.874. J. Biol. Chem. 257, 11922-19931.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11922-19931
    • Lindstedt, S.1    Rundgren, M.2
  • 2
    • 0027177041 scopus 로고
    • Human 4-hydroxyphenylpyruvate dioxygenase. Primary structure and chromosomal localization of the gene
    • Ruetschi, U., Dellsen, A., Sahlin, P., Stenman, G., Rymo, L. & Lindstedt, S. (1993). Human 4-hydroxyphenylpyruvate dioxygenase. Primary structure and chromosomal localization of the gene. Eur. J. Biochem. 213, 1081-1089.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1081-1089
    • Ruetschi, U.1    Dellsen, A.2    Sahlin, P.3    Stenman, G.4    Rymo, L.5    Lindstedt, S.6
  • 3
    • 0028037126 scopus 로고
    • Structure of the human 4-hydroxypyruvic acid dioxygenase gene (Hpd)
    • Awata, H., Endo, F. & Matsuda, I. (1994). Structure of the human 4-hydroxypyruvic acid dioxygenase gene (Hpd). Genomics 23, 534-539.
    • (1994) Genomics , vol.23 , pp. 534-539
    • Awata, H.1    Endo, F.2    Matsuda, I.3
  • 4
    • 0028834746 scopus 로고
    • Regional assignment of the human 4-hydroxyphenylpyruvate dioxygenase gene (Hpd) to 12q24 → qter by fluorescence in situ hybridization
    • Stenman, G., Roijer, E., Ruetschi, U., Dellsen, A., Rymo, L. & Lindstedt, S. (1995). Regional assignment of the human 4-hydroxyphenylpyruvate dioxygenase gene (Hpd) to 12q24 → qter by fluorescence in situ hybridization. Cytogenet. Cell Genet. 71, 374-376.
    • (1995) Cytogenet. Cell Genet. , vol.71 , pp. 374-376
    • Stenman, G.1    Roijer, E.2    Ruetschi, U.3    Dellsen, A.4    Rymo, L.5    Lindstedt, S.6
  • 5
    • 0025828927 scopus 로고
    • Sequences of the mouse F protein alleles and identification of a T cell epitope
    • Shofield, J.P., Vijayakumar, R.K. & Oliveira, D.B.G. (1991). Sequences of the mouse F protein alleles and identification of a T cell epitope. Eur. J. Immunol. 21, 1235-1240.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 1235-1240
    • Shofield, J.P.1    Vijayakumar, R.K.2    Oliveira, D.B.G.3
  • 6
    • 0028939376 scopus 로고
    • A non-sense mutation in the 4-hydroxypyruvic acid dioxygenase gene (Hpd) causes skipping of the constitutive exon and hypertyrosinemia in mouse strain III
    • Endo, F., Awata, H., Katoh, H. & Matsuda, I. (1995). A non-sense mutation in the 4-hydroxypyruvic acid dioxygenase gene (Hpd) causes skipping of the constitutive exon and hypertyrosinemia in mouse strain III. Genomics 25, 164-169.
    • (1995) Genomics , vol.25 , pp. 164-169
    • Endo, F.1    Awata, H.2    Katoh, H.3    Matsuda, I.4
  • 8
    • 0026486822 scopus 로고
    • Primary structure deduced from complementary DNA sequence and expression in cultured cells of mammalian 4-hydroxyphenylpyruvic acid dioxygenase. Evidence that the enzyme is a homodimer of identical subunits homologous to rat liver-specific F alloantigen
    • Endo, F., et al., & Matsuda, I. (1992). Primary structure deduced from complementary DNA sequence and expression in cultured cells of mammalian 4-hydroxyphenylpyruvic acid dioxygenase. Evidence that the enzyme is a homodimer of identical subunits homologous to rat liver-specific F alloantigen. J. Biol. Chem. 267, 24235-24240.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24235-24240
    • Endo, F.1    Matsuda, I.2
  • 9
    • 0011534631 scopus 로고    scopus 로고
    • Cloning of an Arabidopsis thaliana cDNA for p-hydroxyphenylpyruvate dioxygenase (Accession No. U89267)
    • Bartley, G.E., Maxwell, C.A., Wittenbach, V.A. & Scolnik, P.A. (1997). Cloning of an Arabidopsis thaliana cDna for p-hydroxyphenylpyruvate dioxygenase (Accession No. U89267). Plant Physiol. 113, 1463-1465.
    • (1997) Plant Physiol. , vol.113 , pp. 1463-1465
    • Bartley, G.E.1    Maxwell, C.A.2    Wittenbach, V.A.3    Scolnik, P.A.4
  • 10
    • 0030861598 scopus 로고    scopus 로고
    • Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the corresponding cDNA
    • Garcia, I., Rodgers, M., Lenne, C., Rolland, A., Sailland, A. & Matringe, M. (1997). Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the corresponding cDNA. Biochem. J. 325, 761-769.
    • (1997) Biochem. J. , vol.325 , pp. 761-769
    • Garcia, I.1    Rodgers, M.2    Lenne, C.3    Rolland, A.4    Sailland, A.5    Matringe, M.6
  • 11
    • 0029163288 scopus 로고
    • Cloning and expression of a gene encoding a T-cell reactive protein from Coccidioides immitis to 4-hydrophenylpyruvate dioxygenase ad the mammalian F antigen
    • Wyckoff, E.E., Pishko, E.J., Kirkland, T.N. & Cole, G.T. (1995). Cloning and expression of a gene encoding a T-cell reactive protein from Coccidioides immitis to 4-hydrophenylpyruvate dioxygenase ad the mammalian F antigen. Gene 161, 107-111.
    • (1995) Gene , vol.161 , pp. 107-111
    • Wyckoff, E.E.1    Pishko, E.J.2    Kirkland, T.N.3    Cole, G.T.4
  • 13
    • 0027965019 scopus 로고
    • A Streptomyces avermitilis gene encoding a 4-hydroxyphenylpyruvic acid dioxygenase-like protein that directs the production of homogentisic acid and an ochronotic pigment in Escherichia coli
    • Denoya, C.D., Skinner, D.D. & Morgenstern, M.R. (1994). A Streptomyces avermitilis gene encoding a 4-hydroxyphenylpyruvic acid dioxygenase-like protein that directs the production of homogentisic acid and an ochronotic pigment in Escherichia coli. J. Bacteriol. 176, 5312-5319.
    • (1994) J. Bacteriol. , vol.176 , pp. 5312-5319
    • Denoya, C.D.1    Skinner, D.D.2    Morgenstern, M.R.3
  • 15
    • 0027452908 scopus 로고
    • SC-OO51 a 2-benzoyl-cyclohexane-1,3-dione bleaching herbicide, is a potent inhibitor of the enzyme p-hydroxyphenylpyruvate dioxygenase
    • Schulz, A., Oswald, O., Beyer, P. & Kleinig, H. (1993). SC-OO51 a 2-benzoyl-cyclohexane-1,3-dione bleaching herbicide, is a potent inhibitor of the enzyme p-hydroxyphenylpyruvate dioxygenase. FEBS Lett. 318, 162-166.
    • (1993) FEBS Lett. , vol.318 , pp. 162-166
    • Schulz, A.1    Oswald, O.2    Beyer, P.3    Kleinig, H.4
  • 17
    • 0029070081 scopus 로고    scopus 로고
    • Inhibition of 4-hydroxyphenylpyruvate dioxygenase by 2-(2-nitro-4-trifluoromethylbenzoyl)-cyclohexane-1,3-dione and 2-(2-chloro-4-methanesulfonylbenzoyl)-cyclohexane-1,3-dione
    • Ellis, M.K., et al., & Smith, L.L. (1998). Inhibition of 4-hydroxyphenylpyruvate dioxygenase by 2-(2-nitro-4-trifluoromethylbenzoyl)-cyclohexane-1,3-dione and 2-(2-chloro-4-methanesulfonylbenzoyl)-cyclohexane-1,3-dione. Toxicol. Appl. Pharmacol. 133, 12-19.
    • (1998) Toxicol. Appl. Pharmacol. , vol.133 , pp. 12-19
    • Ellis, M.K.1    Smith, L.L.2
  • 18
    • 0026675589 scopus 로고
    • Treatment of hereditary tyrosinemia type I by inhibition of 4-hydroxyphenylpyruvate dioxygenase
    • Lindstedt, S., Holme, E., Lock, E.A., Hjalmarson, O. & Strandvik, B. (1992). Treatment of hereditary tyrosinemia type I by inhibition of 4-hydroxyphenylpyruvate dioxygenase. Lancet 340, 813-817.
    • (1992) Lancet , vol.340 , pp. 813-817
    • Lindstedt, S.1    Holme, E.2    Lock, E.A.3    Hjalmarson, O.4    Strandvik, B.5
  • 19
    • 0033556265 scopus 로고    scopus 로고
    • An archetypical extradiol-cleaving catecholic dioxygenase: The crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2
    • Kita, A., et al., & Miki, K. (1999). An archetypical extradiol-cleaving catecholic dioxygenase: The crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2. Structure 7, 25-34.
    • (1999) Structure , vol.7 , pp. 25-34
    • Kita, A.1    Miki, K.2
  • 20
    • 0028862027 scopus 로고
    • Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading Pseudomonad
    • Han, S., Eltis, L.D., Timmins, K.N., Muchmore, S.W. & Bolin, J.T. (1995). Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading Pseudomonad. Science 270, 976-980.
    • (1995) Science , vol.270 , pp. 976-980
    • Han, S.1    Eltis, L.D.2    Timmins, K.N.3    Muchmore, S.W.4    Bolin, J.T.5
  • 21
    • 0030008087 scopus 로고    scopus 로고
    • Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. Strain KKS102
    • Senda, T., et al., & Mitsui, Y. (1996). Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. Strain KKS102. J. Mol. Biol. 255, 735-752.
    • (1996) J. Mol. Biol. , vol.255 , pp. 735-752
    • Senda, T.1    Mitsui, Y.2
  • 23
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, J.R. (1986). Improved fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, J.R.1
  • 24
    • 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 Crystallogr. D 50, 178-185.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 26
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrix
    • Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrix. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of 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 the location of errors in these models. Acta Crystallogr. A 97, 110-119.
    • (1991) Acta Crystallogr. A , vol.97 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0030590525 scopus 로고    scopus 로고
    • The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity
    • Lee, M.H., Zhang, Z-H., MacKinnon, C.H., Baldwin, J.E. & Crouch, N.P. (1996). The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity. FEBS Lett. 393, 269-272.
    • (1996) FEBS Lett. , vol.393 , pp. 269-272
    • Lee, M.H.1    Zhang, Z.-H.2    MacKinnon, C.H.3    Baldwin, J.E.4    Crouch, N.P.5
  • 30
    • 0028244721 scopus 로고
    • Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering
    • Dumas, P., Bergdoll, M., Cagnon, C. & Masson, J.-M. (1994). Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering. EMBO J. 13, 2483-2492.
    • (1994) EMBO J. , vol.13 , pp. 2483-2492
    • Dumas, P.1    Bergdoll, M.2    Cagnon, C.3    Masson, J.-M.4
  • 31
    • 0030927104 scopus 로고    scopus 로고
    • Crystal structure of human glyoxalase I-evidence for gene duplication and 3D domain swapping
    • Cameron, A.D., Olin, B., Ridderstrom, M., Mannervik, B. & Jones, T.A. (1997). Crystal structure of human glyoxalase I-evidence for gene duplication and 3D domain swapping. EMBO J. 16, 3386-3395.
    • (1997) EMBO J. , vol.16 , pp. 3386-3395
    • Cameron, A.D.1    Olin, B.2    Ridderstrom, M.3    Mannervik, B.4    Jones, T.A.5
  • 32
    • 0032463747 scopus 로고    scopus 로고
    • All in the family: Structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly
    • Bergdoll, M., Eltis, L., Cameron, A.D., Dumas, P. & Bolin, J.T. (1998). All in the family: Structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly. Protein Sci. 7, 1661-1670.
    • (1998) Protein Sci. , vol.7 , pp. 1661-1670
    • Bergdoll, M.1    Eltis, L.2    Cameron, A.D.3    Dumas, P.4    Bolin, J.T.5
  • 34
    • 0000739229 scopus 로고
    • The assay of aromatic amino acid transaminations and keto acid oxidation by enol borate-tautomerase method
    • Lin, E.C.C., Pitt, B.M., Civen, M. & Knox, W.E. (1958). The assay of aromatic amino acid transaminations and keto acid oxidation by enol borate-tautomerase method. J. Biol. Chem. 233, 668-673.
    • (1958) J. Biol. Chem. , vol.233 , pp. 668-673
    • Lin, E.C.C.1    Pitt, B.M.2    Civen, M.3    Knox, W.E.4
  • 35
    • 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. Crystallogr. 24, 409-411.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.H.2
  • 36
    • 85046526624 scopus 로고
    • Evaluation of a single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. (1980). Evaluation of a single-crystal x-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 21, 916-924.
    • (1980) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No4 (1994). The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 38
    • 84943920736 scopus 로고
    • Phase annealing in SHELX-90: Direct methods for larger structures
    • Scheldrick, G. (1990). Phase annealing in SHELX-90: Direct methods for larger structures. Acta Crystallogr. A 46, 467-473.
    • (1990) Acta Crystallogr. A , vol.46 , pp. 467-473
    • Scheldrick, G.1
  • 40
    • 0000449646 scopus 로고
    • Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints
    • Cowtan, K.D & Main, P. (1993). Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints. Acta Crystallogr. D 49, 148-157.
    • (1993) Acta Crystallogr. D , vol.49 , pp. 148-157
    • Cowtan, K.D.1    Main, P.2
  • 41
    • 0026597444 scopus 로고
    • The free-R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. (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.1
  • 42
    • 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. (1993). PROCHECK a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 43
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of molecular structures by the maximum-likelihood method
    • Murshudov, G., Vagin, A.A. & Dodson, E.J. (1997). Refinement of molecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.1    Vagin, A.A.2    Dodson, E.J.3
  • 44
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. & Wilson, K.S. (1993). Automated refinement of protein models. Acta Crystallogr. D 49, 129-147.
    • (1993) Acta Crystallogr. D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 46
    • 33846446220 scopus 로고
    • Restart procedures for the conjugate gradient method
    • Powell, M.J.D. (1977). Restart procedures for the conjugate gradient method. Math. Progr. 12, 241-254.
    • (1977) Math. Progr. , vol.12 , pp. 241-254
    • Powell, M.J.D.1
  • 47
    • 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
  • 48
    • 0030824517 scopus 로고    scopus 로고
    • Ribbons
    • Carson, M. (1997). Ribbons. Methods Enzymol. 277, 493-505.
    • (1997) Methods Enzymol. , vol.277 , pp. 493-505
    • Carson, M.1
  • 49
    • 0032961270 scopus 로고    scopus 로고
    • SPrit: Analysis of multiple sequence alignments in postscript
    • Gouet, P., Courcelle, E., Stuart, D.I. & Metoz, F. (1999). SPrit: Analysis of multiple sequence alignments in postscript. Bioinformatics 15, 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 50
    • 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. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.