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Volumn 345, Issue 5, 2005, Pages 1059-1070

Tracking the evolution of porphobilinogen synthase metal dependence in vitro

Author keywords

crystal structure; evolution; metalloenzyme; porphobilinogen synthase; Pseudomonas aeruginosa

Indexed keywords

ALANINE; AMINO ACID; ASPARTIC ACID; CYSTEINE; ENZYME; ENZYME VARIANT; METAL; PORPHOBILINOGEN SYNTHASE; TETRAPYRROLE DERIVATIVE; ZINC ION;

EID: 11844251357     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.10.053     Document Type: Article
Times cited : (12)

References (27)
  • 1
    • 0002883206 scopus 로고    scopus 로고
    • Chemical synthesis of porphobilinogen and studies of its biosynthesis
    • R. Neier Chemical synthesis of porphobilinogen and studies of its biosynthesis Advan. Nitrogen Heterocycles 2 1996 135 146
    • (1996) Advan. Nitrogen Heterocycles , vol.2 , pp. 135-146
    • Neier, R.1
  • 2
    • 0033528697 scopus 로고    scopus 로고
    • X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 Å resolution
    • P.T. Erskine, E. Norton, J.B. Cooper, R. Lambert, A. Coker, and G. Lewis X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 Å resolution Biochemistry 38 1999 4266 4276
    • (1999) Biochemistry , vol.38 , pp. 4266-4276
    • Erskine, P.T.1    Norton, E.2    Cooper, J.B.3    Lambert, R.4    Coker, A.5    Lewis, G.6
  • 3
    • 0036299038 scopus 로고    scopus 로고
    • Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism
    • F. Frere, W.D. Schubert, F. Stauffer, N. Frankenberg, R. Neier, D. Jahn, and D.W. Heinz Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism J. Mol. Biol. 320 2002 237 247
    • (2002) J. Mol. Biol. , vol.320 , pp. 237-247
    • Frere, F.1    Schubert, W.D.2    Stauffer, F.3    Frankenberg, N.4    Neier, R.5    Jahn, D.6    Heinz, D.W.7
  • 4
    • 0141905850 scopus 로고    scopus 로고
    • Stereochemistry and mechanism of the conversion of 5-aminolevulinic acid into porphobilinogen catalysed by porphobilinogen synthase
    • C.E. Goodwin, and F.J. Leeper Stereochemistry and mechanism of the conversion of 5-aminolevulinic acid into porphobilinogen catalysed by porphobilinogen synthase Org. Biomol. Chem. 1 2003 1443 1446
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 1443-1446
    • Goodwin, C.E.1    Leeper, F.J.2
  • 5
    • 0042569086 scopus 로고    scopus 로고
    • X-ray structure of a putative reaction intermediate of 5-aminolaevulinic acid dehydratase
    • P.T. Erskine, L. Coates, D. Butler, J.H. Youell, A.A. Brindley, and S.P. Wood X-ray structure of a putative reaction intermediate of 5-aminolaevulinic acid dehydratase Biochem. J. 373 2003 733 738
    • (2003) Biochem. J. , vol.373 , pp. 733-738
    • Erskine, P.T.1    Coates, L.2    Butler, D.3    Youell, J.H.4    Brindley, A.A.5    Wood, S.P.6
  • 9
    • 0041318843 scopus 로고    scopus 로고
    • Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase
    • S. Breinig, J. Kervinen, L. Stith, A.S. Wasson, R. Fairman, and A. Wlodawer Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase Nature Struct. Biol. 10 2003 757 763
    • (2003) Nature Struct. Biol. , vol.10 , pp. 757-763
    • Breinig, S.1    Kervinen, J.2    Stith, L.3    Wasson, A.S.4    Fairman, R.5    Wlodawer, A.6
  • 10
    • 0029137828 scopus 로고
    • The structure and evolution of alpha/beta barrel proteins
    • D. Reardon, and G.K. Faber The structure and evolution of alpha/beta barrel proteins FASEB J. 9 1995 497 503
    • (1995) FASEB J. , vol.9 , pp. 497-503
    • Reardon, D.1    Faber, G.K.2
  • 11
    • 0034141656 scopus 로고    scopus 로고
    • The porphobilinogen synthase family of metalloenzymes
    • E.K. Jaffe The porphobilinogen synthase family of metalloenzymes Acta Crystallog. sect. D 56 2000 115 128
    • (2000) Acta Crystallog. Sect. D , vol.56 , pp. 115-128
    • Jaffe, E.K.1
  • 12
    • 0029121431 scopus 로고
    • A mutant Bradyrhizobium japonicum delta-aminolevulinic acid dehydratase with an altered metal requirement functions in situ for tetrapyrrole synthesis in soybean root nodules
    • S. Chauhan, and M.R. O'Brian A mutant Bradyrhizobium japonicum delta-aminolevulinic acid dehydratase with an altered metal requirement functions in situ for tetrapyrrole synthesis in soybean root nodules J. Biol. Chem. 270 1995 19823 19827
    • (1995) J. Biol. Chem. , vol.270 , pp. 19823-19827
    • Chauhan, S.1    O'Brian, M.R.2
  • 13
    • 0027462109 scopus 로고
    • Purification and characterization of 5-aminolaevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain
    • P. Spencer, and P.M. Jordan Purification and characterization of 5-aminolaevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain Biochem. J. 290 1993 279 287
    • (1993) Biochem. J. , vol.290 , pp. 279-287
    • Spencer, P.1    Jordan, P.M.2
  • 14
    • 0037257313 scopus 로고    scopus 로고
    • An unusual phylogenetic variation in the metal ion binding sites of porphobilinogen synthase
    • E.K. Jaffe An unusual phylogenetic variation in the metal ion binding sites of porphobilinogen synthase Chem. Biol. 10 2003 25 34
    • (2003) Chem. Biol. , vol.10 , pp. 25-34
    • Jaffe, E.K.1
  • 15
    • 0029068811 scopus 로고
    • Porphobilinogen synthase, the first source of heme's asymmetry
    • E.K. Jaffe Porphobilinogen synthase, the first source of heme's asymmetry J. Bioenerg. Biomembr. 27 1995 169 179
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 169-179
    • Jaffe, E.K.1
  • 16
    • 0345281626 scopus 로고    scopus 로고
    • 2+-responsive porphobilinogen synthase from Pseudomonas aeruginosa
    • 2+-responsive porphobilinogen synthase from Pseudomonas aeruginosa Biochemistry 38 1999 13968 13975
    • (1999) Biochemistry , vol.38 , pp. 13968-13975
    • Frankenberg, N.1    Heinz, D.W.2    Jahn, D.3
  • 18
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building 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.W.3    Kjeldgaard, M.4
  • 19
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson 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
  • 20
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nature Struct. Biol. 6 1999 458 463
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 21
  • 23
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 24
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • W. Kabsch A solution for the best rotation to relate two sets of vectors Acta Crystallog. sect. A 32 1976 922 923
    • (1976) Acta Crystallog. Sect. a , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P. Kraulis 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.1
  • 26
    • 0029902526 scopus 로고    scopus 로고
    • Comparative studies on the 5-aminolaevulinic acid dehydratases from Pisum sativum, Escherichia coli and Saccharomyces cerevisiae
    • N.M. Senior, K. Brocklehurst, J.B. Cooper, S.P. Wood, P. Erskine, and P.M. Shoolingin-Jordan Comparative studies on the 5-aminolaevulinic acid dehydratases from Pisum sativum, Escherichia coli and Saccharomyces cerevisiae Biochem. J. 320 1996 401 412
    • (1996) Biochem. J. , vol.320 , pp. 401-412
    • Senior, N.M.1    Brocklehurst, K.2    Cooper, J.B.3    Wood, S.P.4    Erskine, P.5    Shoolingin-Jordan, P.M.6
  • 27
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A.T. Brünger 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
    • Brünger, A.T.1


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