메뉴 건너뛰기




Volumn 42, Issue 38, 2003, Pages 11150-11160

NMR studies of the interaction of a type II dihydrofolate reductase with pyridine nucleotides reveal unexpected phosphatase and reductase activity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; AROMATIC COMPOUNDS; CATALYST ACTIVITY; CHEMICAL BONDS; COMPLEXATION; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EID: 0141456387     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0349874     Document Type: Article
Times cited : (20)

References (41)
  • 2
    • 0001596638 scopus 로고
    • Inhibitor binding analysis of dihydrofolate reductases from various species
    • Burchall, J. J., and Hitchings, G. H. (1965) Inhibitor binding analysis of dihydrofolate reductases from various species, Mol. Pharmacol. 1, 126-136.
    • (1965) Mol. Pharmacol. , vol.1 , pp. 126-136
    • Burchall, J.J.1    Hitchings, G.H.2
  • 3
    • 0015514652 scopus 로고
    • Trimethoprim resistance determined by R factors
    • Fleming, M. P., Datta, N., and Gruneberg, R. N. (1972) Trimethoprim resistance determined by R factors, Br. Med. J. 1, 726-728.
    • (1972) Br. Med. J. , vol.1 , pp. 726-728
    • Fleming, M.P.1    Datta, N.2    Gruneberg, R.N.3
  • 4
    • 0017597814 scopus 로고
    • Two distinct types of trimethoprim-resistant dihydrofolate reductase specified by R-plasmids of different compatibility groups
    • Pattishall, K. H., Acar, J., Burchall, J. J., Goldstein, F. W., and Harvey, R. J. (1977) Two Distinct Types of Trimethoprim-resistant Dihydrofolate Reductase Specified by R-Plasmids of Different Compatibility Groups, J. Biol. Chem. 252, 2319-2323.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2319-2323
    • Pattishall, K.H.1    Acar, J.2    Burchall, J.J.3    Goldstein, F.W.4    Harvey, R.J.5
  • 6
    • 0018638966 scopus 로고
    • The amino acid sequence of the trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67
    • Stone, D., and Smith, S. L. (1979) The Amino Acid Sequence of the Trimethoprim-resistant Dihydrofolate Reductase Specified in Escherichia coli by R-Plasmid R67, J. Biol. Chem. 254, 10857-10861.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10857-10861
    • Stone, D.1    Smith, S.L.2
  • 12
    • 0025175189 scopus 로고
    • Characterization and stereochemistry of cofactor oxidation by a type II dihydrofolate reductase
    • Brito, R. M. M., Reddick, R., Bennett, G. N., Rudolph, F. B., and Rosevear, P. R. (1990) Characterization and Stereochemistry of Cofactor Oxidation by a Type II Dihydrofolate Reductase, Biochemistry 29, 9825-9831.
    • (1990) Biochemistry , vol.29 , pp. 9825-9831
    • Brito, R.M.M.1    Reddick, R.2    Bennett, G.N.3    Rudolph, F.B.4    Rosevear, P.R.5
  • 13
    • 0026328118 scopus 로고
    • Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of the N-terminus in the protein
    • Reece, L. J., Nichols, R., Ogden, R. C., and Howell, E. E. (1991) Construction of a synthetic gene for an R-plasmid-encoded dihydrofolate reductase and studies on the role of the N-terminus in the protein, Biochemistry 30, 10895-10904.
    • (1991) Biochemistry , vol.30 , pp. 10895-10904
    • Reece, L.J.1    Nichols, R.2    Ogden, R.C.3    Howell, E.E.4
  • 14
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D. R., and Kay, L. E. (1994) Gradient-Enhanced Triple-Resonance Three-Dimensional NMR Experiments with Improved Sensitivity, J. Magn. Reson., Ser. B 103, 203-216.
    • (1994) J. Magn. Reson., Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 16
    • 0027568083 scopus 로고
    • A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments
    • Logan, T. M., Olejniczak, E. T., Xu, R. X., and Fesik, S. W. (1993) A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments, J. Biomol. NMR 3, 225-231.
    • (1993) J. Biomol. NMR , vol.3 , pp. 225-231
    • Logan, T.M.1    Olejniczak, E.T.2    Xu, R.X.3    Fesik, S.W.4
  • 18
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 19
    • 34249765651 scopus 로고
    • NMR View: A computer-program for the visualization and analysis of NMR data
    • Johnson, B. A., and Blevins, R. A. (1994) NMR View: a computer-program for the visualization and analysis of NMR data, J. Biomol. NMR 4, 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 20
    • 0037469137 scopus 로고    scopus 로고
    • Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium
    • Pari, K., Mueller, G. A., DeRose, E. F., Kirby, T. W., and London, R. E. (2003) Solution Structure of the RNase H Domain of the HIV-1 Reverse Transcriptase in the Presence of Magnesium, Biochemistry 42, 639-650.
    • (2003) Biochemistry , vol.42 , pp. 639-650
    • Pari, K.1    Mueller, G.A.2    DeRose, E.F.3    Kirby, T.W.4    London, R.E.5
  • 21
    • 0032511359 scopus 로고    scopus 로고
    • 15N chemical shift anisotropy relaxation interference: Unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules
    • 15N Chemical Shift Anisotropy Relaxation Interference: Unambiguous Determination of Rotational Diffusion Tensors and Chemical Exchange Effects in Biological Macromolecules, J. Am. Chem. Soc. 120, 7905-7915.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7905-7915
    • Kroenke, C.D.1    Loria, J.P.2    Lee, L.K.3    Rance, M.4    Palmer, A.G.5
  • 22
    • 0029550886 scopus 로고
    • Rotational diffusion anisotropy of human ubiquitin from N-15 NMR relaxation
    • Tjandra, N., Feller, S. E., Pastor, R. W., and Bax, A. (1995) Rotational Diffusion Anisotropy of Human Ubiquitin from N-15 NMR Relaxation, J. Am. Chem. Soc. 117, 12562-12566.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 12562-12566
    • Tjandra, N.1    Feller, S.E.2    Pastor, R.W.3    Bax, A.4
  • 23
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A. M., Akke, M., and Palmer, A. G., III (1995) Backbone Dynamics of Escherichia coli Ribonuclease HI: Correlations with Structure and Function in an Active Enzyme, J. Mol. Biol. 246, 144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer A.G. III3
  • 24
    • 0037266991 scopus 로고    scopus 로고
    • The use of model selection in the model-free analysis of protein dynamics
    • d'Auvergne, E. J., and Gooley, P. R. (2003). The use of model selection in the model-free analysis of protein dynamics, J. Biomol. NMR 25, 25-39.
    • (2003) J. Biomol. NMR , vol.25 , pp. 25-39
    • D'Auvergne, E.J.1    Gooley, P.R.2
  • 25
    • 0028393784 scopus 로고
    • The C-13 Chemical-Shift Index: A simple method for the identification of protein secondary structure using C-13 chemical-shift data
    • Wishart, D. S., and Sykes, B. D. (1994) The C-13 Chemical-Shift Index: a simple method for the identification of protein secondary structure using C-13 chemical-shift data, J. Biomol. NMR 4, 171-180.
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 26
    • 0016137358 scopus 로고
    • 13C magnetic resonance study of the ionization of N-acetyl-DL-proline in aqueous solution
    • 13C magnetic resonance study of the ionization of N-acetyl-DL-proline in aqueous solution, Biochim. Biophys. Acta 343, 656-662.
    • (1974) Biochim. Biophys. Acta , vol.343 , pp. 656-662
    • Bedford, G.R.1    Sadler, P.J.2
  • 27
    • 0032522713 scopus 로고    scopus 로고
    • Local control of peptide conformation: Stabilization of cis proline peptide bonds by aromatic proline interactions
    • Wu, W. J., and Raleigh, D. P. (1998) Local Control of Peptide Conformation: Stabilization of cis Proline Peptide Bonds by Aromatic Proline Interactions, Biopolymers 45, 381-394.
    • (1998) Biopolymers , vol.45 , pp. 381-394
    • Wu, W.J.1    Raleigh, D.P.2
  • 28
    • 2242480182 scopus 로고    scopus 로고
    • Kinetic analysis of R67 dihydrofolate reductase folding: From the unfolded monomer to the native tetramer
    • Bodenreider, C., Kellershohn, N., Goldberg, M. E., and Mejean, A. (2002) Kinetic Analysis of R67 Dihydrofolate Reductase Folding: From the Unfolded Monomer to the Native Tetramer, Biochemistry 41, 14988-14999.
    • (2002) Biochemistry , vol.41 , pp. 14988-14999
    • Bodenreider, C.1    Kellershohn, N.2    Goldberg, M.E.3    Mejean, A.4
  • 29
    • 0035732844 scopus 로고    scopus 로고
    • One site fits both: A model for the ternary complex of folate + NADPH in R67 dihydrofolate reductase, a D2 symmetric enzyme
    • Howell, E. E., Shukla, U., Hicks, S. N., Smiley, R. D., Kuhn, L. A., and Zavodsky, M. I. (2001) One site fits both: a model for the ternary complex of folate + NADPH in R67 dihydrofolate reductase, a D2 symmetric enzyme, J. Comput.-Aided Mol. Des. 15, 1035-1052.
    • (2001) J. Comput.-Aided Mol. Des. , vol.15 , pp. 1035-1052
    • Howell, E.E.1    Shukla, U.2    Hicks, S.N.3    Smiley, R.D.4    Kuhn, L.A.5    Zavodsky, M.I.6
  • 30
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage λ N-peptide/boxB RNA complex
    • Zwahlen, C., Legault, P., Vincent, S. J. F., Greenblatt, J., Konrat, R., and Kay, L. E. (1997) Methods for Measurement of Intermolecular NOEs by Multinuclear NMR Spectroscopy: Application to a Bacteriophage λ N-Peptide/boxB RNA Complex, J. Am. Chem. Soc. 119, 6711-6721.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6711-6721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.J.F.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6
  • 32
    • 0029875239 scopus 로고    scopus 로고
    • On transition structures for hydride transfer step: A theoretical study of the reaction catalyzed by dihydrofolate reductase enzyme
    • Andres, J., Moliner, V., Safont, V. S., Domingo, L. R., Picher, M. T., and Krechl, J. (1996) On transition structures for hydride transfer step: A theoretical study of the reaction catalyzed by dihydrofolate reductase enzyme, Bioorg. Chem. 24, 10-18.
    • (1996) Bioorg. Chem. , vol.24 , pp. 10-18
    • Andres, J.1    Moliner, V.2    Safont, V.S.3    Domingo, L.R.4    Picher, M.T.5    Krechl, J.6
  • 33
    • 0023655438 scopus 로고
    • + phosphatase: A novel mitochondrial enzyme
    • + Phosphatase: A Novel Mitochondrial Enzyme, Biochem. Biophys. Res. Commun. 146, 253-257.
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 253-257
    • Richter, C.1
  • 34
    • 0343090409 scopus 로고    scopus 로고
    • Evidence of active NADP(+) phosphatase in dormant seeds of Avena sativa L.
    • Gallais, S., de Crescenzo, M. A. P., and Laval-Martin, D. L. (2000) Evidence of active NADP(+) phosphatase in dormant seeds of Avena sativa L., J. Exp. Bot. 51, 1389-1394.
    • (2000) J. Exp. Bot. , vol.51 , pp. 1389-1394
    • Gallais, S.1    De Crescenzo, M.A.P.2    Laval-Martin, D.L.3
  • 35
    • 0025118811 scopus 로고
    • Ultrastructural distribution of NADPase within the golgi-apparatus and lysosomes of mammalian-cells
    • Smith, C. E., Hermo, L., Fazel, A., Lalli, M. F., and Bergeron, J. J. M. (1990), Ultrastructural Distribution of NADPase Within the Golgi-Apparatus and Lysosomes of Mammalian-Cells, Prog. Histochem. Cytochem. 21, 1-124.
    • (1990) Prog. Histochem. Cytochem. , vol.21 , pp. 1-124
    • Smith, C.E.1    Hermo, L.2    Fazel, A.3    Lalli, M.F.4    Bergeron, J.J.M.5
  • 36
    • 0035949449 scopus 로고    scopus 로고
    • Role of S65, Q67, I68, and Y69 residues in homotetrameric R67 dihydrofolate reductase
    • Strader, M. B., Smiley, R. D., Stinnett, L. G., VerBerkmoes, N. C., and Howell, E. E. (2001) Role of S65, Q67, I68, and Y69 residues in homotetrameric R67 dihydrofolate reductase, Biochemistry 40, 11344-11352.
    • (2001) Biochemistry , vol.40 , pp. 11344-11352
    • Strader, M.B.1    Smiley, R.D.2    Stinnett, L.G.3    VerBerkmoes, N.C.4    Howell, E.E.5
  • 37
    • 0008759140 scopus 로고
    • α-pyridine nucleotides as substrates for a plasmid-specified dihydrofolate reductase
    • Smith, S. L., and Burchall, J. J. (1983) α-Pyridine nucleotides as substrates for a plasmid-specified dihydrofolate reductase, Proc. Natl. Acad. Sci. U.S.A. 80, 4619-4623.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 4619-4623
    • Smith, S.L.1    Burchall, J.J.2
  • 38
    • 0035928796 scopus 로고    scopus 로고
    • Backbone dynamics in dihydrofolate reductase complexes: Role of loop flexibility in the catalytic mechanism
    • Osborne, M. J., Schnell, J., Benkovic, S. J., Dyson, H. J., and Wright, P. E. (2001) Backbone Dynamics in Dihydrofolate Reductase Complexes: Role of Loop Flexibility in the Catalytic Mechanism, Biochemistry 40, 9846-9859.
    • (2001) Biochemistry , vol.40 , pp. 9846-9859
    • Osborne, M.J.1    Schnell, J.2    Benkovic, S.J.3    Dyson, H.J.4    Wright, P.E.5
  • 39
    • 0037159205 scopus 로고    scopus 로고
    • Coupling interactions of distal residues enhance dihydrofolate reductase catalysis: Mutational effects on hydride transfer rates
    • Rajagopalan, P. T. R., Lutz, S., and Benkovic, S. J. (2002) Coupling Interactions of Distal Residues Enhance Dihydrofolate Reductase Catalysis: Mutational Effects on Hydride Transfer Rates, Biochemistry 41, 12618-12628.
    • (2002) Biochemistry , vol.41 , pp. 12618-12628
    • Rajagopalan, P.T.R.1    Lutz, S.2    Benkovic, S.J.3
  • 41
    • 0031687653 scopus 로고    scopus 로고
    • Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design
    • Liang, J., Edelbrunner, H., and Woodward, C. (1998) Anatomy of Protein Pockets and Cavities: Measurement of Binding Site Geometry and Implications for Ligand Design, Protein Sci. 7, 1884-1897.
    • (1998) Protein Sci. , vol.7 , pp. 1884-1897
    • Liang, J.1    Edelbrunner, H.2    Woodward, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.