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Volumn 252, Issue 1, 1998, Pages 51-58

Structural studies of histidine-containing phosphocarrier protein from Enterococcus faecalis

Author keywords

Histidine containing phosphocarrier protein; NMR; Phosphotransferase system

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; HISTIDINE; PHOSPHOPROTEIN;

EID: 0032520183     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2520051.x     Document Type: Article
Times cited : (8)

References (40)
  • 1
    • 0015240448 scopus 로고
    • Purification and properties of a phosphocarrier protein (HPr) of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli
    • Anderson, B., Weigel, N., Kundig, W. & Roseman, S. (1971) Purification and properties of a phosphocarrier protein (HPr) of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli, J. Biol. Chem. 246, 7023-7033.
    • (1971) J. Biol. Chem. , vol.246 , pp. 7023-7033
    • Anderson, B.1    Weigel, N.2    Kundig, W.3    Roseman, S.4
  • 2
    • 0020479924 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system. Isolation and characterization of a phosphocarrier protein HPr from wild type and mutants of Salmonella typhimurium
    • Beneski, D. A., Nakazawa, A., Weigel, N., Hartman, P. E. & Roseman, S. (1982) Sugar transport by the bacterial phosphotransferase system. Isolation and characterization of a phosphocarrier protein HPr from wild type and mutants of Salmonella typhimurium, J. Biol. Chem. 257, 24492-24498.
    • (1982) J. Biol. Chem. , vol.257 , pp. 24492-24498
    • Beneski, D.A.1    Nakazawa, A.2    Weigel, N.3    Hartman, P.E.4    Roseman, S.5
  • 3
    • 0028199768 scopus 로고
    • Sequence and expression of the genes for HPr (ptsH) and enzyme I (ptsI) of the phosphoenopyruvate-dependent phosphotransferase transport system from Streptococcus mutatis
    • Boyd, D. A., Cvitkovitch, D. G. & Hamilton, I. R. (1994) Sequence and expression of the genes for HPr (ptsH) and enzyme I (ptsI) of the phosphoenopyruvate-dependent phosphotransferase transport system from Streptococcus mutatis, Infect. Immun. 62, 1156-1165.
    • (1994) Infect. Immun. , vol.62 , pp. 1156-1165
    • Boyd, D.A.1    Cvitkovitch, D.G.2    Hamilton, I.R.3
  • 4
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L. & Ernst, R. R. (1983) Coherence transfer by isotropic mixing: application to proton correlation spectroscopy, J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 5
    • 0020851355 scopus 로고
    • ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr. a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes
    • Deutscher, J. & Saier, M. H. (1983) ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr. a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes, Proc. Natl Acad. Sci. USA 80, 6790-6794.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 6790-6794
    • Deutscher, J.1    Saier, M.H.2
  • 6
    • 0022979375 scopus 로고
    • Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: Amino acid sequence and site of ATP-dependent phosphorylation of HPr
    • Deutscher, J., Pevec, B., Beyreuther, K., Kiltz, H.-H. & Hengstenherg, W. (1986) Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: amino acid sequence and site of ATP-dependent phosphorylation of HPr. Biochemistry 25, 6543-6551.
    • (1986) Biochemistry , vol.25 , pp. 6543-6551
    • Deutscher, J.1    Pevec, B.2    Beyreuther, K.3    Kiltz, H.-H.4    Hengstenherg, W.5
  • 7
    • 0027743009 scopus 로고
    • Phosphotransferase system of Streptococcus salivarius: Characterization of the ptsH gene and its products
    • Gagnon, G., Vadeboncoeur, C. & Frenette, M. (1993) Phosphotransferase system of Streptococcus salivarius: characterization of the ptsH gene and its products, Gene (Amst.) 136, 27-34.
    • (1993) Gene (Amst.) , vol.136 , pp. 27-34
    • Gagnon, G.1    Vadeboncoeur, C.2    Frenette, M.3
  • 8
    • 0029665424 scopus 로고    scopus 로고
    • Conformational transitions in p2lras and in its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP
    • Geyer, M., Schweins, S., Herrmann, C., Prisner, T., Wittinghofer, A. & Kalbitzer, H. R. (1996) Conformational transitions in p2lras and in its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP, Biochemistry 35, 10308-10320.
    • (1996) Biochemistry , vol.35 , pp. 10308-10320
    • Geyer, M.1    Schweins, S.2    Herrmann, C.3    Prisner, T.4    Wittinghofer, A.5    Kalbitzer, H.R.6
  • 9
    • 0031557402 scopus 로고    scopus 로고
    • Cooperative and non-cooperative DNA binding modes of catabolic control protein CcpH from Bacillus megaterium result from sensing two different signals
    • Gösseringer, R., Küster, E., Galinier, A., Deutscher, J. & Hillen, W. (1997) Cooperative and non-cooperative DNA binding modes of catabolic control protein CcpH from Bacillus megaterium result from sensing two different signals, J. Mol. Biol. 266, 665-676.
    • (1997) J. Mol. Biol. , vol.266 , pp. 665-676
    • Gösseringer, R.1    Küster, E.2    Galinier, A.3    Deutscher, J.4    Hillen, W.5
  • 11
    • 0014561151 scopus 로고
    • Phosphotransferase system of Staphylococcus aureus: Its requirement for the accumulation and metabolism of galactosides
    • Hengstenberg, W., Penberthy, W. K., Kill, K. L. & Morse, M. L. (1969) Phosphotransferase system of Staphylococcus aureus: its requirement for the accumulation and metabolism of galactosides, J. Bacteriol. 99, 383-388.
    • (1969) J. Bacteriol. , vol.99 , pp. 383-388
    • Hengstenberg, W.1    Penberthy, W.K.2    Kill, K.L.3    Morse, M.L.4
  • 12
    • 0026534155 scopus 로고
    • Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0Å resolution
    • Herzberg, O., Reddy, P., Sutrina, S., Saier, M. H., Reizer, J. & Kapadia, G. (1992) Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0Å resolution, Proc. Natl Acad. Sci. USA 89, 2499-2503.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2499-2503
    • Herzberg, O.1    Reddy, P.2    Sutrina, S.3    Saier, M.H.4    Reizer, J.5    Kapadia, G.6
  • 14
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B. H., Bachmann, P. & Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy, J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 15
    • 0027340388 scopus 로고
    • The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination
    • Jia, Z., Quail, J. W., Waygood, E. B. & Delbaere, L. T. (1993) The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination, J. Biol. Chem. 268, 22490-22501.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22490-22501
    • Jia, Z.1    Quail, J.W.2    Waygood, E.B.3    Delbaere, L.T.4
  • 16
    • 0028056155 scopus 로고
    • The 1.6 Å structure of the histidine-containing phosphocarrier protein HPr from Streptococcus faecalis
    • Jia, Z., Vandonselaar, M., Hengstenberg, W., Quail, J. W. & Delbaere, L. T. J. (1994) The 1.6 Å structure of the histidine-containing phosphocarrier protein HPr from Streptococcus faecalis, J. Mol. Biol. 236, 1341-1355.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1341-1355
    • Jia, Z.1    Vandonselaar, M.2    Hengstenberg, W.3    Quail, J.W.4    Delbaere, L.T.J.5
  • 17
    • 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
  • 18
    • 0020477463 scopus 로고
    • Hpr proteins of different microorganisms studied by hydrogen-1 high resolution nuclear magnetic resonance: Similarities of structures and mechanisms
    • Kalbitzer, H. R., Hengstenberg, W., Rösch, P., Muss, P., Bernsmann, P., Engelmann, R., Dörschug, M. & Deutscher, J. (1982) Hpr proteins of different microorganisms studied by hydrogen-1 high resolution nuclear magnetic resonance: similarities of structures and mechanisms, Biochemistry 21, 2879-2885.
    • (1982) Biochemistry , vol.21 , pp. 2879-2885
    • Kalbitzer, H.R.1    Hengstenberg, W.2    Rösch, P.3    Muss, P.4    Bernsmann, P.5    Engelmann, R.6    Dörschug, M.7    Deutscher, J.8
  • 20
    • 12244297937 scopus 로고
    • Vicinal proton coupling in nuclear magnetic resonance
    • Karplus, M. (1963) Vicinal proton coupling in nuclear magnetic resonance, J. Am. Chem. Soc. 85, 2870-2871.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 2870-2871
    • Karplus, M.1
  • 21
    • 0022925241 scopus 로고
    • 1H-NMR studies of histidine-containing protein from E. coli - Secondary and tertiary structure determined by NMR
    • 1H-NMR studies of histidine-containing protein from E. coli - secondary and tertiary structure determined by NMR, Biochemistry 25, 7774-7781.
    • (1986) Biochemistry , vol.25 , pp. 7774-7781
    • Klevit, R.E.1    Waygood, E.B.2
  • 22
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wüthrich, K. J. (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.J.3
  • 23
    • 0027232148 scopus 로고
    • Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein Hpr of the phosphoenolpyruvate-dependant phosphotransferase system of Staphylococcus carnosus: Site-directed mutagenesis with the ptsH gene, biochemical characterisation and NMR studies of the mutant proteins
    • Kruse, R., Hengstenberg, W., Beneicke, W. & Kalbitzer, H. R. (1993) Involvement of various amino- and carboxyl-terminal residues in the active site of the histidine-containing protein Hpr of the phosphoenolpyruvate-dependant phosphotransferase system of Staphylococcus carnosus: site-directed mutagenesis with the ptsH gene, biochemical characterisation and NMR studies of the mutant proteins, Protein Eng. 6, 417-423.
    • (1993) Protein Eng. , vol.6 , pp. 417-423
    • Kruse, R.1    Hengstenberg, W.2    Beneicke, W.3    Kalbitzer, H.R.4
  • 24
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskovski, 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. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskovski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 0021114895 scopus 로고
    • Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins
    • Marion, D. &. Wüthrieh, K. (1983) Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins, Biochem. Biophys. Res. Commun. 113, 967-974.
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrieh, K.2
  • 27
    • 0017194757 scopus 로고
    • The phosphoenolpyruvate: Methyl-alpha-D-glucoside phosphotransferase system in Bacillus subtilis Marburg 168: purification and identification of the phosphocarrier protein (HPr)
    • Marquet, M., Creignou, M.-C. & Dedonder, R. (1976) The phosphoenolpyruvate: methyl-alpha-D-glucoside phosphotransferase system in Bacillus subtilis Marburg 168: purification and identification of the phosphocarrier protein (HPr). Biochemistry 58, 435-441.
    • (1976) Biochemistry , vol.58 , pp. 435-441
    • Marquet, M.1    Creignou, M.-C.2    Dedonder, R.3
  • 30
    • 0029645286 scopus 로고
    • Structural evidence for the evolutionary divergence of mycoplasma from gram-positive bacteria: The histidine-containing phosphocarrier protein
    • Pieper, U., Kapadia, G., Zhu, P. P., Peterkofsky, A. & Herzberg, O. (1995) Structural evidence for the evolutionary divergence of mycoplasma from gram-positive bacteria: the histidine-containing phosphocarrier protein, Structure (Lond.) 3, 781-790.
    • (1995) Structure (Lond.) , vol.3 , pp. 781-790
    • Pieper, U.1    Kapadia, G.2    Zhu, P.P.3    Peterkofsky, A.4    Herzberg, O.5
  • 31
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase system in bacteria
    • Postma, P. W., Lengeler, J. W. & Jacobson, G. R. (1993) Phosphoenolpyruvate: carbohydrate phosphotransferase system in bacteria, Microbiol. Rev. 57, 543-594.
    • (1993) Microbiol. Rev. , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 33
    • 0024121605 scopus 로고
    • Evidence for the presence of heat-stable protein (HPr) and ATP-dependent HPr kinase in heterofermentative lactobacilli lacking phosphoeno/pyruvate:glycose phosphotransferase activity
    • Reizer, J., Peterowsky, A. & Romano, A. (1988) Evidence for the presence of heat-stable protein (HPr) and ATP-dependent HPr kinase in heterofermentative lactobacilli lacking phosphoeno/pyruvate:glycose phosphotransferase activity, Proc. Natl Acad. Sci. USA 85, 2041-2045.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2041-2045
    • Reizer, J.1    Peterowsky, A.2    Romano, A.3
  • 34
    • 0000492963 scopus 로고
    • Broadband homonuclear cross polarization in 2D N. M. R. using DIPSI-2
    • Rucker, S. P. & Shaka, A. J. (1989) Broadband homonuclear cross polarization in 2D N. M. R. using DIPSI-2, Mol. Phys. 68, 509-517.
    • (1989) Mol. Phys. , vol.68 , pp. 509-517
    • Rucker, S.P.1    Shaka, A.J.2
  • 35
    • 0029039486 scopus 로고
    • Protein phosphorylation and the regulation of carbon metabolism: Comparisons in gram-positive versus gram-negative bacteria
    • Saier, M. H., Chavaux, S., Deutscher, V., Reizer, J. & Ye, J. J. (1995) Protein phosphorylation and the regulation of carbon metabolism: comparisons in gram-positive versus gram-negative bacteria, Trends. Biochem. Sci. 20, 267-271.
    • (1995) Trends. Biochem. Sci. , vol.20 , pp. 267-271
    • Saier, M.H.1    Chavaux, S.2    Deutscher, V.3    Reizer, J.4    Ye, J.J.5
  • 36
    • 0017152197 scopus 로고
    • Mycoplasma phosphoenolpyruvate-dependent sugar phosphotransferase system: Purification and characterization of the phosphocarrier protein
    • Ullah, A. H. & Cirillo, V. P. (1976) Mycoplasma phosphoenolpyruvate-dependent sugar phosphotransferase system: purification and characterization of the phosphocarrier protein, J. Bacteriol. 127, 1298-1306.
    • (1976) J. Bacteriol. , vol.127 , pp. 1298-1306
    • Ullah, A.H.1    Cirillo, V.P.2
  • 37
    • 0028905499 scopus 로고
    • High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data
    • Van Nuland, N. A. J., Boelens, R., Scheck, R. M. & Robillard, G. T. (1995) High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data, J. Mol. Biol. 246, 180-193.
    • (1995) J. Mol. Biol. , vol.246 , pp. 180-193
    • Van Nuland, N.A.J.1    Boelens, R.2    Scheck, R.M.3    Robillard, G.T.4
  • 38
    • 0000883197 scopus 로고
    • Nonselective three-dimensional NMR spectroscopy. The 3D NOE-HOHAHA experiment
    • Vuister, G. W., Boelens, R. & Kaptein, R. (1988) Nonselective three-dimensional NMR spectroscopy. The 3D NOE-HOHAHA experiment, J. Magn. Reson. 80, 176-185.
    • (1988) J. Magn. Reson. , vol.80 , pp. 176-185
    • Vuister, G.W.1    Boelens, R.2    Kaptein, R.3
  • 40
    • 0027098199 scopus 로고
    • Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy
    • Wittekind, M., Rajagopal, P., Branchini, B. R., Reizer, J., Saier, M. H. & Klevit, R. E. (1992) Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy, Protein Sci. 1, 1363-1376.
    • (1992) Protein Sci. , vol.1 , pp. 1363-1376
    • Wittekind, M.1    Rajagopal, P.2    Branchini, B.R.3    Reizer, J.4    Saier, M.H.5    Klevit, R.E.6


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