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Volumn 289, Issue 3, 1999, Pages 591-602

High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase

Author keywords

Crystal structure; Metal binding; Porphobilinogen synthase; Pseudomonas aeruginosa; Tetrapyrrole biosynthesis

Indexed keywords

LEVULINIC ACID; LYSINE; MAGNESIUM ION; NITROGEN; PORPHOBILINOGEN SYNTHASE; SCHIFF BASE; SOLVENT;

EID: 0033546125     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2808     Document Type: Article
Times cited : (75)

References (39)
  • 1
    • 0026014150 scopus 로고
    • Aminolevulinic acid dehydratase in pea (Pisum sativum L.)
    • Boese, Q. F., Spano, A. J., Li, J. & Timko, M. P. (1991). Aminolevulinic acid dehydratase in pea (Pisum sativum L.). J. Biol. Chem. 266, 17060-17066.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17060-17066
    • Boese, Q.F.1    Spano, A.J.2    Li, J.3    Timko, M.P.4
  • 2
    • 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
  • 4
    • 0029121431 scopus 로고
    • A mutant Bradyrhzobium japonicum δ-aminolevulinic acid dehydratase with an altered metal requirement functions in situ for tetrapyrrole synthesis in soybean root nodules
    • Chauhan, S. & O'Brian, M. R. (1995). A mutant Bradyrhizobium japonicum δ-aminolevulinic acid dehydratase with an altered metal requirement functions in situ for tetrapyrrole synthesis in soybean root nodules. J. Biol. Chem. 270, 19823-19827.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19823-19827
    • Chauhan, S.1    O'Brian, M.R.2
  • 5
    • 0031039339 scopus 로고    scopus 로고
    • Characterization of a recombinant pea 5-aminolevulinic acid dehydratase and comparative inhibition studies with the Escherichiacoli dehydratase
    • Cheung, K.-M., Spencer, P., Timko, M. P. & Shoolingin-Jordan, P. M. (1997). Characterization of a recombinant pea 5-aminolevulinic acid dehydratase and comparative inhibition studies with the Escherichiacoli dehydratase. Biochemistry, 36, 1148-1156.
    • (1997) Biochemistry , vol.36 , pp. 1148-1156
    • Cheung, K.-M.1    Spencer, P.2    Timko, M.P.3    Shoolingin-Jordan, P.M.4
  • 10
    • 0031888801 scopus 로고    scopus 로고
    • Cloning, mapping and functional characterization of the hemB gene of Pseudomonas aeruginosa, which encodes a magnesium-dependent 5-aminolevulinic acid dehydratase
    • Frankenberg, N., Kittel, T., Hungerer, C., Römling, U. & Jahn, D. (1998). Cloning, mapping and functional characterization of the hemB gene of pseudomonas aeruginosa, which encodes a magnesium-dependent 5-aminolevulinic acid dehydratase. Mol. Gen. Genet. 257, 485-489.
    • (1998) Mol. Gen. Genet. , vol.257 , pp. 485-489
    • Frankenberg, N.1    Kittel, T.2    Hungerer, C.3    Römling, U.4    Jahn, D.5
  • 12
    • 0029068811 scopus 로고
    • Porphobilinogen synthase, the first source of heme's asymmetry
    • Jaffe, E. K. (1995). Porphobilinogen synthase, the first source of heme's asymmetry. J. Bioenerg. Biomembr. 27, 169-179.
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 169-179
    • Jaffe, E.K.1
  • 13
    • 0028173334 scopus 로고
    • 13C]levulinic acid modification of mammalian and bacterial porphobilinogen synthase suggests an active site containing two Zn(II)
    • 13C]levulinic acid modification of mammalian and bacterial porphobilinogen synthase suggests an active site containing two Zn(II). Biochemistry, 33, 11554-11562.
    • (1994) Biochemistry , vol.33 , pp. 11554-11562
    • Jaffe, E.K.1    Volin, M.2    Myers, C.B.3    Abrams, W.R.4
  • 14
    • 0028933309 scopus 로고
    • Characterization of the role of the stimulatory magnesium of Escherichia coli porphobilinogen synthase
    • Jaffe, E. K., Ali, S., Mitchell, L. W., Taylor, K. M., Volin, M. & Markham, G. D. (1995). Characterization of the role of the stimulatory magnesium of Escherichia coli porphobilinogen synthase. Biochemistry, 34, 244-251.
    • (1995) Biochemistry , vol.34 , pp. 244-251
    • Jaffe, E.K.1    Ali, S.2    Mitchell, L.W.3    Taylor, K.M.4    Volin, M.5    Markham, G.D.6
  • 15
    • 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 Crystallog. Sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 16
    • 0001794011 scopus 로고
    • The biosynthesis of 5-aminolaevulinic acid and its transformation into uroporphobilinogen III
    • (Jordan, P. M., ed.), Elsevier, Amsterdam
    • Jordan, P. M. (1991). The biosynthesis of 5-aminolaevulinic acid and its transformation into uroporphobilinogen III. In Biosynthesis of Tetrapyrroles (Jordan, P. M., ed.), pp. 1-47, Elsevier, Amsterdam.
    • (1991) Biosynthesis of Tetrapyrroles , pp. 1-47
    • Jordan, P.M.1
  • 17
    • 0028603602 scopus 로고
    • Highlights in haem biosynthesis
    • Jordan, P. M. (1994). Highlights in haem biosynthesis. Curr. Opin. Struc. Biol. 4, 902-911.
    • (1994) Curr. Opin. Struc. Biol. , vol.4 , pp. 902-911
    • Jordan, P.M.1
  • 18
    • 85046526624 scopus 로고
    • Evaluation of single crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. (1988). Evaluation of single crystal X-ray diffraction data from a position-sensitive detector. Acta Crystallog. Sect. A, 21, 916-924.
    • (1988) Acta Crystallog. Sect. A , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 19
    • 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
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots or protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots or protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V. S. & Wilson, K. S. (1993). Automated refinement of protein models. Acta Crystallog. Sect. D, 49, 129-147.
    • (1993) Acta Crystallog. Sect. D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 22
    • 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. Crystallog. 26, 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
  • 24
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B. W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 25
    • 0028057108 scopus 로고
    • Raster3D version 2.0: A program for photorealistic molecular graphics
    • Merrit, E. A. & Murphy, M. E. P. (1994). Raster3D version 2.0: A program for photorealistic molecular graphics. Acta Crystallog. Sect. D, 50, 869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 26
    • 0027326081 scopus 로고
    • Phorphobilinogen synthase from Escherichia coli is a Zn(II) metalloenzyme stimulated by Mg(II)
    • Mitchell, L. W. & Jaffe, E. K. (1993). Phorphobilinogen synthase from Escherichia coli is a Zn(II) metalloenzyme stimulated by Mg(II). Arch. Biochem. Biophys. 300, 169-177.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 169-177
    • Mitchell, L.W.1    Jaffe, E.K.2
  • 27
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A. & Dodson, E. H. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. Sect. D, 53, 240-255.
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.H.3
  • 28
    • 0015694174 scopus 로고
    • δ-Aminolevulinic acid dehydratase of Rhodopseudomonas capsulata
    • Nandi, D. L. & Shemin, D. (1973). δ-Aminolevulinic acid dehydratase of Rhodopseudomonas capsulata. Arch. Biochem. Biophys. 158, 305-311.
    • (1973) Arch. Biochem. Biophys. , vol.158 , pp. 305-311
    • Nandi, D.L.1    Shemin, D.2
  • 29
    • 0014429272 scopus 로고
    • δ-Aminolevulinic acid dehydratase of Rhodopseudomonas spheroides
    • Nandi, D. L., Baker-Cohen, K. F. & Shemin, D. (1968). δ-Aminolevulinic acid dehydratase of Rhodopseudomonas spheroides. J. Biol. Chem. 243, 1224-1230.
    • (1968) J. Biol. Chem. , vol.243 , pp. 1224-1230
    • Nandi, D.L.1    Baker-Cohen, K.F.2    Shemin, D.3
  • 30
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: An automated package for molecular replacement. Acta Crystallog. Sect. A, 50, 157-163.
    • (1994) Acta Crystallog. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 31
    • 0030735358 scopus 로고    scopus 로고
    • Magnetic resonance studies on the active site and metal centers of Bradyrhizobium japonicum porphobilinogen synthase
    • Petrovich, R. M. & Jaffe, E. K. (1997). Magnetic resonance studies on the active site and metal centers of Bradyrhizobium japonicum porphobilinogen synthase. Biochemistry, 36, 13421-13427.
    • (1997) Biochemistry , vol.36 , pp. 13421-13427
    • Petrovich, R.M.1    Jaffe, E.K.2
  • 32
    • 0029994635 scopus 로고    scopus 로고
    • Bradyrhizobium japonicum porphobilinogen synthase uses two Mg(II) and monovalent cations
    • Petrovich, R. M., Litwin, S. & Jaffe, E. K. (1996). Bradyrhizobium japonicum porphobilinogen synthase uses two Mg(II) and monovalent cations. J. Biol. Chem. 271, 8692-8699.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8692-8699
    • Petrovich, R.M.1    Litwin, S.2    Jaffe, E.K.3
  • 33
    • 0029137828 scopus 로고
    • The structure and evolution of alpha/beta barrel proteins
    • Reardon, D. & Farber, G. K. (1995). The structure and evolution of alpha/beta barrel proteins. FASEB J. 9, 497-503.
    • (1995) FASEB J. , vol.9 , pp. 497-503
    • Reardon, D.1    Farber, G.K.2
  • 35
    • 0028830064 scopus 로고
    • Characterization of the two 5-aminolaevulinic acid binding sites, the A- and P-sites, of 5-aminolaevulinic acid dehydratase from Escherichia coli
    • Spencer, P. & Jordan, P. M. (1995). Characterization of the two 5-aminolaevulinic acid binding sites, the A- and P-sites, of 5-aminolaevulinic acid dehydratase from Escherichia coli. Biochem. J. 305, 151-158.
    • (1995) Biochem. J. , vol.305 , pp. 151-158
    • Spencer, P.1    Jordan, P.M.2
  • 36
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994). CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22, 4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 39
    • 0342985266 scopus 로고
    • Human delta-aminolevulinate dehydratase: Nucleotide sequence of a full-length cDNA clone
    • Wetmur, J. G., Bishop, D. F., Cantelmo, C. & Desnik, R. J. (1986). Human delta-aminolevulinate dehydratase: Nucleotide sequence of a full-length cDNa clone. Proc. Natl Acad. Sci. USA, 83, 7703-7707.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 7703-7707
    • Wetmur, J.G.1    Bishop, D.F.2    Cantelmo, C.3    Desnik, R.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.