메뉴 건너뛰기




Volumn 184, Issue 3, 2013, Pages 438-444

High-resolution crystal structure of the eukaryotic HMP-P synthase (THIC) from Arabidopsis thaliana

Author keywords

HMP P synthase; Metal binding site; SAM radical dependent enzyme; Thiamin biosynthesis; X ray structure

Indexed keywords

4 AMINO 5 HYDROXYMETHYL 2 METHYLPYRIMIDINE PHOSPHATE SYNTHASE; BACTERIAL ENZYME; COBALT; SYNTHETASE; UNCLASSIFIED DRUG; ZINC ION;

EID: 84888039165     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2013.10.005     Document Type: Article
Times cited : (20)

References (36)
  • 1
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: a comprehensive python-based system for macromolecular structure solution
    • Adams P.D., et al. PHENIX: a comprehensive python-based system for macromolecular structure solution. Acta. Crystallogr. D Biol. Crystallogr. 2010, 66(Pt 2):213-221.
    • (2010) Acta. Crystallogr. D Biol. Crystallogr. , vol.66 , Issue.PART. 2 , pp. 213-221
    • Adams, P.D.1
  • 2
    • 33846342197 scopus 로고    scopus 로고
    • The metabolic response of heterotrophic Arabidopsis cells to oxidative stress
    • Baxter C.J., et al. The metabolic response of heterotrophic Arabidopsis cells to oxidative stress. Plant Physiol. 2007, 143(1):312-325.
    • (2007) Plant Physiol. , vol.143 , Issue.1 , pp. 312-325
    • Baxter, C.J.1
  • 3
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
    • Berkovitch F., Nicolet Y., Wan J.T., Jarrett J.T., Drennan C.L. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 2004, 303(5654):76-79.
    • (2004) Science , vol.303 , Issue.5654 , pp. 76-79
    • Berkovitch, F.1    Nicolet, Y.2    Wan, J.T.3    Jarrett, J.T.4    Drennan, C.L.5
  • 4
    • 65549167312 scopus 로고    scopus 로고
    • Thiamin diphosphate in biological chemistry: new aspects of thiamin metabolism, especially triphosphate derivatives acting other than as cofactors
    • Bettendorff L., Wins P. Thiamin diphosphate in biological chemistry: new aspects of thiamin metabolism, especially triphosphate derivatives acting other than as cofactors. FEBS J. 2009, 276(11):2917-2925.
    • (2009) FEBS J. , vol.276 , Issue.11 , pp. 2917-2925
    • Bettendorff, L.1    Wins, P.2
  • 5
    • 78149460648 scopus 로고    scopus 로고
    • A "radical dance" in thiamin biosynthesis: mechanistic analysis of the bacterial hydroxymethylpyrimidine phosphate synthase
    • Chatterjee A., Hazra A.B., Abdelwahed S., Hilmey D.G., Begley T.P. A "radical dance" in thiamin biosynthesis: mechanistic analysis of the bacterial hydroxymethylpyrimidine phosphate synthase. Angew. Chem. Int. Ed. Engl. 2010, 49(46):8653-8656.
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , Issue.46 , pp. 8653-8656
    • Chatterjee, A.1    Hazra, A.B.2    Abdelwahed, S.3    Hilmey, D.G.4    Begley, T.P.5
  • 6
    • 33744932425 scopus 로고    scopus 로고
    • Thiamin biosynthesis in eukaryotes: characterization of the enzyme-bound product of thiazole synthase from Saccharomyces cerevisiae and its implications in thiazole biosynthesis
    • Chatterjee A., Jurgenson C.T., Schroeder F.C., Ealick S.E., Begley T.P. Thiamin biosynthesis in eukaryotes: characterization of the enzyme-bound product of thiazole synthase from Saccharomyces cerevisiae and its implications in thiazole biosynthesis. J. Am. Chem. Soc. 2006, 128(22):7158-7159.
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.22 , pp. 7158-7159
    • Chatterjee, A.1    Jurgenson, C.T.2    Schroeder, F.C.3    Ealick, S.E.4    Begley, T.P.5
  • 7
    • 33947204418 scopus 로고    scopus 로고
    • Biosynthesis of thiamin thiazole in eukaryotes: conversion of NAD to an advanced intermediate
    • Chatterjee A., Jurgenson C.T., Schroeder F.C., Ealick S.E., Begley T.P. Biosynthesis of thiamin thiazole in eukaryotes: conversion of NAD to an advanced intermediate. J. Am. Chem. Soc. 2007, 129(10):2914-2922.
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.10 , pp. 2914-2922
    • Chatterjee, A.1    Jurgenson, C.T.2    Schroeder, F.C.3    Ealick, S.E.4    Begley, T.P.5
  • 9
    • 84871333510 scopus 로고    scopus 로고
    • The last piece in the vitamin B1 biosynthesis puzzle: structural and functional insight into yeast 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P) synthase
    • Coquille S., Roux C., Fitzpatrick T.B., Thore S. The last piece in the vitamin B1 biosynthesis puzzle: structural and functional insight into yeast 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P) synthase. J. Biol. Chem. 2012, 287(50):42333-42343.
    • (2012) J. Biol. Chem. , vol.287 , Issue.50 , pp. 42333-42343
    • Coquille, S.1    Roux, C.2    Fitzpatrick, T.B.3    Thore, S.4
  • 10
    • 13444263350 scopus 로고    scopus 로고
    • Solution structure of the E. coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain
    • Deprez C., Lloubes R., Gavioli M., Marion D., Guerlesquin F., Blanchard L. Solution structure of the E. coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain. J. Mol. Biol. 2005, 346(4):1047-1057.
    • (2005) J. Mol. Biol. , vol.346 , Issue.4 , pp. 1047-1057
    • Deprez, C.1    Lloubes, R.2    Gavioli, M.3    Marion, D.4    Guerlesquin, F.5    Blanchard, L.6
  • 11
    • 33747103795 scopus 로고    scopus 로고
    • A connection between iron and sulfur cluster metabolism and the biosynthesis of 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate in Salmonella enterica
    • Dougherty M.J., Downs D.M. A connection between iron and sulfur cluster metabolism and the biosynthesis of 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate in Salmonella enterica. Microbiology 2006, 152(Pt 8):2345-2353.
    • (2006) Microbiology , vol.152 , Issue.PART. 8 , pp. 2345-2353
    • Dougherty, M.J.1    Downs, D.M.2
  • 12
    • 84866021687 scopus 로고    scopus 로고
    • Structural diversity in the AdoMet radical enzyme superfamily
    • Dowling D.P., Vey J.L., Croft A.K., Drennan C.L. Structural diversity in the AdoMet radical enzyme superfamily. Biochim. Biophys. Acta 2012, 11(1824):1178-1195.
    • (2012) Biochim. Biophys. Acta , vol.11 , Issue.1824 , pp. 1178-1195
    • Dowling, D.P.1    Vey, J.L.2    Croft, A.K.3    Drennan, C.L.4
  • 13
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Pt 1
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 2004, 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , Issue.PART. 12 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 14
    • 0034912671 scopus 로고    scopus 로고
    • Radical mechanisms of enzymatic catalysis
    • Frey P.A. Radical mechanisms of enzymatic catalysis. Annu. Rev. Biochem. 2001, 70:121-148.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 121-148
    • Frey, P.A.1
  • 15
    • 40949116404 scopus 로고    scopus 로고
    • The direct precursor of the pyrimidine moiety of thiamin is not urocanic acid but histidine in Saccharomyces cerevisiae
    • Ishida S., Tazuya-Murayama K., Kijima Y., Yamada K. The direct precursor of the pyrimidine moiety of thiamin is not urocanic acid but histidine in Saccharomyces cerevisiae. J. Nutr. Sci. Vitaminol. (Tokyo) 2008, 54(1):7-10.
    • (2008) J. Nutr. Sci. Vitaminol. (Tokyo) , vol.54 , Issue.1 , pp. 7-10
    • Ishida, S.1    Tazuya-Murayama, K.2    Kijima, Y.3    Yamada, K.4
  • 16
    • 67650729745 scopus 로고    scopus 로고
    • The structural and biochemical foundations of thiamin biosynthesis
    • Jurgenson C.T., Begley T.P., Ealick S.E. The structural and biochemical foundations of thiamin biosynthesis. Annu. Rev. Biochem. 2009, 78:569-603.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 569-603
    • Jurgenson, C.T.1    Begley, T.P.2    Ealick, S.E.3
  • 17
    • 33748803376 scopus 로고    scopus 로고
    • Structural insights into the function of the thiamin biosynthetic enzyme Thi4 from Saccharomyces cerevisiae
    • Jurgenson C.T., Chatterjee A., Begley T.P., Ealick S.E. Structural insights into the function of the thiamin biosynthetic enzyme Thi4 from Saccharomyces cerevisiae. Biochemistry 2006, 45(37):11061-11070.
    • (2006) Biochemistry , vol.45 , Issue.37 , pp. 11061-11070
    • Jurgenson, C.T.1    Chatterjee, A.2    Begley, T.P.3    Ealick, S.E.4
  • 19
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: a case study using the phyre server
    • Kelley L.A., Sternberg M.J. Protein structure prediction on the web: a case study using the phyre server. Nat. Protoc. 2009, 4(3):363-371.
    • (2009) Nat. Protoc. , vol.4 , Issue.3 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 20
    • 34547107087 scopus 로고    scopus 로고
    • Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro
    • Kriek M., Martins F., Leonardi R., Fairhurst S.A., Lowe D.J., Roach P.L. Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro. J. Biol. Chem. 2007, 282(24):17413-17423.
    • (2007) J. Biol. Chem. , vol.282 , Issue.24 , pp. 17413-17423
    • Kriek, M.1    Martins, F.2    Leonardi, R.3    Fairhurst, S.A.4    Lowe, D.J.5    Roach, P.L.6
  • 21
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372(3):774-797.
    • (2007) J. Mol. Biol. , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 22
    • 84861879091 scopus 로고    scopus 로고
    • Thiamin pyrimidine biosynthesis in Candida albicans: a remarkable reaction between histidine and pyridoxal phosphate
    • Lai R.Y., et al. Thiamin pyrimidine biosynthesis in Candida albicans: a remarkable reaction between histidine and pyridoxal phosphate. J. Am. Chem. Soc. 2012, 134(22):9157-9159.
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.22 , pp. 9157-9159
    • Lai, R.Y.1
  • 23
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 1993, 231(4):1049-1067.
    • (1993) J. Mol. Biol. , vol.231 , Issue.4 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 24
    • 4744361651 scopus 로고    scopus 로고
    • Biosynthesis of the thiamin pyrimidine: the reconstitution of a remarkable rearrangement reaction
    • Lawhorn B.G., Mehl R.A., Begley T.P. Biosynthesis of the thiamin pyrimidine: the reconstitution of a remarkable rearrangement reaction. Org. Biomol. Chem. 2004, 2(17):2538-2546.
    • (2004) Org. Biomol. Chem. , vol.2 , Issue.17 , pp. 2538-2546
    • Lawhorn, B.G.1    Mehl, R.A.2    Begley, T.P.3
  • 25
    • 50849098497 scopus 로고    scopus 로고
    • ThiC is an [Fe-S] cluster protein that requires AdoMet to generate the 4-amino-5-hydroxymethyl-2-methylpyrimidine moiety in thiamin synthesis
    • Martinez-Gomez N.C., Downs D.M. ThiC is an [Fe-S] cluster protein that requires AdoMet to generate the 4-amino-5-hydroxymethyl-2-methylpyrimidine moiety in thiamin synthesis. Biochemistry 2008, 47(35):9054-9056.
    • (2008) Biochemistry , vol.47 , Issue.35 , pp. 9054-9056
    • Martinez-Gomez, N.C.1    Downs, D.M.2
  • 29
    • 0028263799 scopus 로고
    • + encodes a 6-cysteine zinc finger-containing transcription factor that regulates the nmt1 promoter in fission yeast
    • + encodes a 6-cysteine zinc finger-containing transcription factor that regulates the nmt1 promoter in fission yeast. J. Biol. Chem. 1994, 269(16):11921-11926.
    • (1994) J. Biol. Chem. , vol.269 , Issue.16 , pp. 11921-11926
    • Tang, C.S.1    Bueno, A.2    Russell, P.3
  • 31
    • 33847635732 scopus 로고    scopus 로고
    • S-adenosylmethionine as an oxidant: the radical SAM superfamily
    • Wang S.C., Frey P.A. S-adenosylmethionine as an oxidant: the radical SAM superfamily. Trends Biochem. Sci. 2007, 32(3):101-110.
    • (2007) Trends Biochem. Sci. , vol.32 , Issue.3 , pp. 101-110
    • Wang, S.C.1    Frey, P.A.2
  • 32
    • 0037804259 scopus 로고    scopus 로고
    • The THI5 gene family of Saccharomyces cerevisiae: distribution of homologues among the hemiascomycetes and functional redundancy in the aerobic biosynthesis of thiamin from pyridoxine
    • Wightman R., Meacock P.A. The THI5 gene family of Saccharomyces cerevisiae: distribution of homologues among the hemiascomycetes and functional redundancy in the aerobic biosynthesis of thiamin from pyridoxine. Microbiology 2003, 149(Pt 6):1447-1460.
    • (2003) Microbiology , vol.149 , Issue.PART. 6 , pp. 1447-1460
    • Wightman, R.1    Meacock, P.A.2
  • 33
    • 0037206833 scopus 로고    scopus 로고
    • Thiamine derivatives bind messenger RNAs directly to regulate bacterial gene expression
    • Winkler W., Nahvi A., Breaker R.R. Thiamine derivatives bind messenger RNAs directly to regulate bacterial gene expression. Nature 2002, 419(6910):952-956.
    • (2002) Nature , vol.419 , Issue.6910 , pp. 952-956
    • Winkler, W.1    Nahvi, A.2    Breaker, R.R.3
  • 34
    • 77951581676 scopus 로고    scopus 로고
    • Large-scale domain dynamics and adenosylcobalamin reorientation orchestrate radical catalysis in ornithine 4,5-aminomutase
    • Wolthers K.R., Levy C., Scrutton N.S., Leys D. Large-scale domain dynamics and adenosylcobalamin reorientation orchestrate radical catalysis in ornithine 4,5-aminomutase. J. Biol. Chem. 2010, 285(18):13942-13950.
    • (2010) J. Biol. Chem. , vol.285 , Issue.18 , pp. 13942-13950
    • Wolthers, K.R.1    Levy, C.2    Scrutton, N.S.3    Leys, D.4
  • 35
    • 0142183433 scopus 로고    scopus 로고
    • Biosynthesis of vitamin B1 in yeast. Derivation of the pyrimidine unit from pyridoxine and histidine. Intermediacy of urocanic acid
    • Zeidler J., Sayer B.G., Spenser I.D. Biosynthesis of vitamin B1 in yeast. Derivation of the pyrimidine unit from pyridoxine and histidine. Intermediacy of urocanic acid. J. Am. Chem. Soc. 2003, 125(43):13094-13105.
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.43 , pp. 13094-13105
    • Zeidler, J.1    Sayer, B.G.2    Spenser, I.D.3
  • 36
    • 0030883568 scopus 로고    scopus 로고
    • Identification of a DNA element in the fission yeast Schizosaccharomyces pombe nmt1 (thi3) promoter involved in thiamine-regulated gene expression
    • Zurlinden A., Schweingruber M.E. Identification of a DNA element in the fission yeast Schizosaccharomyces pombe nmt1 (thi3) promoter involved in thiamine-regulated gene expression. J. Bacteriol. 1997, 179(18):5956-5958.
    • (1997) J. Bacteriol. , vol.179 , Issue.18 , pp. 5956-5958
    • Zurlinden, A.1    Schweingruber, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.