메뉴 건너뛰기




Volumn 186, Issue 21, 2004, Pages 7134-7140

Crystal structure of the YgfZ protein from Escherichia coli suggests a folate-dependent regulatory role in one-carbon metabolism

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; BETAINE; CARBON; DIMETHYLGLYCINE; DIMETHYLGLYCINE OXIDASE; FOLIC ACID; GENE PRODUCT; GLYCINE CLEAVAGE SYSTEM; OXIDOREDUCTASE; PROTEIN YGFZ; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 6044267984     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.21.7134-7140.2004     Document Type: Article
Times cited : (33)

References (38)
  • 3
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D Biol. Crystallogr. 50:760-763.
    • (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 4
    • 0347323165 scopus 로고    scopus 로고
    • The CCR4-NOT complex plays diverse roles in mRNA metabolism
    • Denis, C. L., and J. Chen. 2003. The CCR4-NOT complex plays diverse roles in mRNA metabolism. Prog. Nucleic Acid Res. Mol. Biol. 73:221-250.
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.73 , pp. 221-250
    • Denis, C.L.1    Chen, J.2
  • 7
    • 0034873892 scopus 로고    scopus 로고
    • GcvR interacts with GcvA to inhibit activation of the Escherichia coli glycine cleavage operon
    • Ghrist, A. C., G. Heil, and G. V. Stauffer. 2001. GcvR interacts with GcvA to inhibit activation of the Escherichia coli glycine cleavage operon. Microbiology 147:2215-2221.
    • (2001) Microbiology , vol.147 , pp. 2215-2221
    • Ghrist, A.C.1    Heil, G.2    Stauffer, G.V.3
  • 8
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Multiple sequence alignments in PostScript
    • Gouet, P., E. Courcelle, D. I. Stuart, and F. Metoz. 1999. ESPript: 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
  • 9
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm, L., and C. Sander. 1998. Touring protein fold space with Dali/FSSP. Nucleic Acids Res. 26:316-319.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 10
    • 0033537865 scopus 로고    scopus 로고
    • Control of expression of one-carbon metabolism genes of Saccharomyces cerevisiae is mediated by a tetrahydrofolate-responsive protein binding to a glycine regulatory region including a core 5′-CTTCTT-3′ motif
    • Hong, S. P., M. D. Piper, D. A. Sinclair, and I. W. Dawes. 1999. Control of expression of one-carbon metabolism genes of Saccharomyces cerevisiae is mediated by a tetrahydrofolate-responsive protein binding to a glycine regulatory region including a core 5′-CTTCTT-3′ motif. J. Biol. Chem. 274:10523-10532.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10523-10532
    • Hong, S.P.1    Piper, M.D.2    Sinclair, D.A.3    Dawes, I.W.4
  • 11
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in these models
    • Jones, T. A., J. Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A 47:110-119.
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 12
    • 0015937406 scopus 로고
    • The glycine cleavage system: Composition, reaction mechanism, and physiological significance
    • Kikuchi, G. 1973. The glycine cleavage system: composition, reaction mechanism, and physiological significance. Mol. Cell. Biochem. 1:169-187.
    • (1973) Mol. Cell. Biochem. , vol.1 , pp. 169-187
    • Kikuchi, G.1
  • 13
    • 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
  • 14
    • 0041465718 scopus 로고    scopus 로고
    • Channelling and formation of 'active' formaldehyde in dimethylglycine oxidase
    • Leys, D., J. Basran, and N. S. Scrutton. 2003. Channelling and formation of 'active' formaldehyde in dimethylglycine oxidase. EMBO J. 22:4038-4048.
    • (2003) EMBO J. , vol.22 , pp. 4038-4048
    • Leys, D.1    Basran, J.2    Scrutton, N.S.3
  • 15
    • 0033808685 scopus 로고    scopus 로고
    • Folic acid: Nutritional biochemistry, molecular biology, and role in disease processes
    • Lucock, M. 2000. Folic acid: nutritional biochemistry, molecular biology, and role in disease processes. Mol. Genet. Metab. 71:121-138.
    • (2000) Mol. Genet. Metab. , vol.71 , pp. 121-138
    • Lucock, M.1
  • 16
    • 0005506691 scopus 로고
    • The metabolism of dimethylglycine by liver mitochondria
    • MacKenzie, C. G., and W. R. Frisell. 1958. The metabolism of dimethylglycine by liver mitochondria. J. Biol. Chem. 232:417-427.
    • (1958) J. Biol. Chem. , vol.232 , pp. 417-427
    • MacKenzie, C.G.1    Frisell, W.R.2
  • 17
    • 0000992903 scopus 로고    scopus 로고
    • One-carbon metabolism
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.). American Society for Microbiology, Washington, D.C.
    • Matthews, M. G. 1996. One-carbon metabolism, p. 600-611. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, 2nd Ed. , pp. 600-611
    • Matthews, M.G.1
  • 18
    • 0017383955 scopus 로고
    • Mutants of formyltetrahydrofolate interconversion pathway of Saccharomyces cerevisiae
    • McKenzie, K. Q., and E. W. Jones. 1977. Mutants of formyltetrahydrofolate interconversion pathway of Saccharomyces cerevisiae. Genetics 86:85-102.
    • (1977) Genetics , vol.86 , pp. 85-102
    • McKenzie, K.Q.1    Jones, E.W.2
  • 19
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A., and D. J. Bacon. 1997. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 20
    • 0034832015 scopus 로고    scopus 로고
    • Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp.: Implications for glycine betaine catabolism
    • Meskys, R., R. J. Harris, V. Casaite, J. Basran, and N. S. Scrutton. 2001. Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp.: implications for glycine betaine catabolism. Eur. J. Biochem. 268:3390-3398.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3390-3398
    • Meskys, R.1    Harris, R.J.2    Casaite, V.3    Basran, J.4    Scrutton, N.S.5
  • 21
    • 0035252680 scopus 로고    scopus 로고
    • Transcription factors: Global and detailed views
    • Muller, C. W. 2001. Transcription factors: global and detailed views. Curr. Opin. Struct. Biol. 11:26-32.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 26-32
    • Muller, C.W.1
  • 23
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., S. E. Brenner, T. Hubbard, and C. Chothia. 1995. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 24
    • 0028923757 scopus 로고
    • Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts in Escherichia coli
    • Nagy, P. L., A. Marolewski, S. J. Benkovic, and H. Zalkin. 1995. Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts in Escherichia coli. J. Bacteriol. 177:1292-1298.
    • (1995) J. Bacteriol. , vol.177 , pp. 1292-1298
    • Nagy, P.L.1    Marolewski, A.2    Benkovic, S.J.3    Zalkin, H.4
  • 25
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., K. A. Sharp, and B. Honig. 1991. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 27
    • 0020478515 scopus 로고
    • Purification and characterization of chicken liver T-protein, a component of the glycine cleavage system
    • Okamura-Ikeda, K., K. Fujiwara, and Y. Motokawa. 1982. Purification and characterization of chicken liver T-protein, a component of the glycine cleavage system. J. Biol. Chem. 257:135-139.
    • (1982) J. Biol. Chem. , vol.257 , pp. 135-139
    • Okamura-Ikeda, K.1    Fujiwara, K.2    Motokawa, Y.3
  • 28
    • 0027326195 scopus 로고
    • Cloning and nucleotide sequence of the gcv operon encoding the Escherichia coli glycine-cleavage system
    • Okamura-Ikeda, K., Y. Ohmura, K. Fujiwara, and Y. Motokawa. 1993. Cloning and nucleotide sequence of the gcv operon encoding the Escherichia coli glycine-cleavage system. Eur. J. Biochem. 216:539-548.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 539-548
    • Okamura-Ikeda, K.1    Ohmura, Y.2    Fujiwara, K.3    Motokawa, Y.4
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0018850362 scopus 로고
    • Formyl-methenyl-methylenetetrahydrofolate synthetase (combined): A multifunctional protein in eukaryotic folate metabolism
    • Paukert, J. L., and J. C. Rabinowitz. 1980. Formyl-methenyl- methylenetetrahydrofolate synthetase (combined): a multifunctional protein in eukaryotic folate metabolism. Methods Enzymol. 66:616-626.
    • (1980) Methods Enzymol. , vol.66 , pp. 616-626
    • Paukert, J.L.1    Rabinowitz, J.C.2
  • 31
    • 0034613194 scopus 로고    scopus 로고
    • Regulation of the balance of one-carbon metabolism in Saccharomyces cerevisiae
    • Piper, M. D., S. P. Hong, G. E. Ball, and I. W. Dawes. 2000. Regulation of the balance of one-carbon metabolism in Saccharomyces cerevisiae. J. Biol. Chem. 275:30987-30995.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30987-30995
    • Piper, M.D.1    Hong, S.P.2    Ball, G.E.3    Dawes, I.W.4
  • 32
    • 0000262153 scopus 로고
    • Serine hydroxymethyltransferase
    • R. L. Blakley and S. J. Benkovic (ed.), John Wiley & Sons, New York, N.Y.
    • Schirch, L. 1984. Serine hydroxymethyltransferase, p. 399-431. In R. L. Blakley and S. J. Benkovic (ed.), Folates and pterins, vol. 1. John Wiley & Sons, New York, N.Y.
    • (1984) Folates and Pterins , vol.1 , pp. 399-431
    • Schirch, L.1
  • 33
    • 0028226494 scopus 로고
    • Characterization of the Escherichia coli gcv operon
    • Stauffer, L. T., S. J. Fogarty, and G. V. Stauffer. 1994. Characterization of the Escherichia coli gcv operon. Gene 142:17-22.
    • (1994) Gene , vol.142 , pp. 17-22
    • Stauffer, L.T.1    Fogarty, S.J.2    Stauffer, G.V.3
  • 34
    • 0028029968 scopus 로고
    • Characterization of the gcv control region from Escherichia coli
    • Stauffer, L. T., and G. V. Stauffer. 1994. Characterization of the gcv control region from Escherichia coli. J. Bacteriol. 176:6159-6164.
    • (1994) J. Bacteriol. , vol.176 , pp. 6159-6164
    • Stauffer, L.T.1    Stauffer, G.V.2
  • 35
    • 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., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.