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Volumn 76, Issue 2-3, 1998, Pages 359-367

The structure and function of HPr

Author keywords

HPr; NMR; Phosphoenolpyruvate:sugar phosphotransferase system; Phosphohistidine; Phosphoserine

Indexed keywords

ASPARAGINE; GUANIDINE; HISTIDINE; PHOSPHOENOLPYRUVATE; PHOSPHOSERINE; PHOSPHOTRANSFERASE; SERINE; THREONINE;

EID: 0032453554     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o98-043     Document Type: Review
Times cited : (18)

References (53)
  • 1
    • 0015240448 scopus 로고
    • Sugar transport. III. Purification and properties of a phosphocarrier protein (HPr) of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli
    • Anderson, B., Weigel, N., Kundig, W., and Roseman, S. 1971. Sugar transport. III. 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
    • 0026074966 scopus 로고
    • Involvement of the carboxy-terminal residue in the active site of histidine-containing protein, HPr, of the phosphoenolpyruvate:Sugar phosphotransferase system of Escherichia coli
    • Anderson, J.W., Bhanot, P., Georges, F., Klevit, R.E., and Waygood, E.B. 1991. Involvement of the carboxy-terminal residue in the active site of histidine-containing protein, HPr, of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli. Biochemistry, 30: 9601-9607.
    • (1991) Biochemistry , vol.30 , pp. 9601-9607
    • Anderson, J.W.1    Bhanot, P.2    Georges, F.3    Klevit, R.E.4    Waygood, E.B.5
  • 3
    • 0026830659 scopus 로고
    • Properties of phosphorylated protein intermediates of the bacterial phosphoenolpyruvate:Sugar phosphotransferase system
    • Anderson, J.W., Saier, M.H., Jr., Reizer, J., and Waygood, E.B. 1992. Properties of phosphorylated protein intermediates of the bacterial phosphoenolpyruvate:sugar phosphotransferase system. Biochem. Cell Biol. 70: 242-246.
    • (1992) Biochem. Cell Biol. , vol.70 , pp. 242-246
    • Anderson, J.W.1    Saier M.H., Jr.2    Reizer, J.3    Waygood, E.B.4
  • 4
    • 0027163002 scopus 로고
    • The involvement of the arginine-17 residue in the active site of the histidine-containing protein, HPr, of the phosphoenolpyruvate:Sugar phosphotransferase system of Escherichia coli
    • Anderson, J.W., Pullen, K., Georges, F., Klevit, R.E., and Waygood, E.B. 1993. The involvement of the arginine-17 residue in the active site of the histidine-containing protein, HPr, of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli. J. Biol. Chem. 268: 12 325-12 333.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12325-12333
    • Anderson, J.W.1    Pullen, K.2    Georges, F.3    Klevit, R.E.4    Waygood, E.B.5
  • 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., and Saier, M.H., Jr. 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. U.S.A. 80: 6790-6794.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 6790-6794
    • Deutscher, J.1    Saier M.H., Jr.2
  • 6
    • 0024410821 scopus 로고
    • Regulatory functions of the phosphocarrier protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system in gram-positive bacteria
    • Deutscher, J., Sossna, G., and Treboul, G.G. 1989. Regulatory functions of the phosphocarrier protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system in gram-positive bacteria. FEMS Microbiol. Rev. 63: 167-174.
    • (1989) FEMS Microbiol. Rev. , vol.63 , pp. 167-174
    • Deutscher, J.1    Sossna, G.2    Treboul, G.G.3
  • 7
    • 0018308740 scopus 로고
    • Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system. Copurification of HPr and 1-6 glucan
    • Dooijewaard, G., Roossien, F.F., and Robillard, G.T. 1979. Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system. Copurification of HPr and 1-6 glucan. Biochemistry, 18: 2990-2996.
    • (1979) Biochemistry , vol.18 , pp. 2990-2996
    • Dooijewaard, G.1    Roossien, F.F.2    Robillard, G.T.3
  • 8
    • 0023665020 scopus 로고
    • Tertiary structure of histidine-containing protein of the phosphoenolpyruvate:Sugar phosphotransferase system of Escherichia coli
    • El-Kabbani, O.A.L., Waygood, E.B., and Delbaere, L.T.J. 1987. Tertiary structure of histidine-containing protein of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli. J. Biol. Chem. 262: 12 926-12 929.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12926-12929
    • El-Kabbani, O.A.L.1    Waygood, E.B.2    Delbaere, L.T.J.3
  • 10
    • 0026351817 scopus 로고
    • New resonance assignments for the histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy do not alter the proposed folding topology
    • Hammen, P.K., Waygood, E.B., and Klevit, R.E. 1991. New resonance assignments for the histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy do not alter the proposed folding topology. Biochemistry, 30: 11 842-11 850.
    • (1991) Biochemistry , vol.30 , pp. 11842-11850
    • Hammen, P.K.1    Waygood, E.B.2    Klevit, R.E.3
  • 11
    • 0028587898 scopus 로고
    • Unraveling a bacterial hexose transport pathway
    • Herzberg, O., and Klevit, R. 1994. Unraveling a bacterial hexose transport pathway. Curr. Opin. Struct. Biol. 4: 814-822.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 814-822
    • Herzberg, O.1    Klevit, R.2
  • 12
    • 0026534155 scopus 로고
    • Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0 Å resolution
    • Herzberg, O., Reddy, P., Reizer, J., and Kapadia, G. 1992. Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0 Å resolution. Proc. Natl. Acad. Sci. U.S.A. 89: 2499-2503.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2499-2503
    • Herzberg, O.1    Reddy, P.2    Reizer, J.3    Kapadia, G.4
  • 13
    • 0027340388 scopus 로고
    • The 2.0-Å resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr
    • Jia, Z., Quail, J.W., Waygood, E.B., and Delbaere, L.T.J. 1993a. The 2.0-Å resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. J. Biol. Chem. 268: 22 490-22 501.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22490-22501
    • Jia, Z.1    Quail, J.W.2    Waygood, E.B.3    Delbaere, L.T.J.4
  • 14
    • 0027458493 scopus 로고
    • Active-centre torsion-angle strain revealed in 1.6 Å-resolution structure of histidine-containing phosphocarrier protein
    • Jia, Z., Vandonselaar, M., Quail, W., and Delbaere, L.T.J. 1993b. Active-centre torsion-angle strain revealed in 1.6 Å-resolution structure of histidine-containing phosphocarrier protein. Nature (London), 361: 94-97.
    • (1993) Nature (London) , vol.361 , pp. 94-97
    • Jia, Z.1    Vandonselaar, M.2    Quail, W.3    Delbaere, L.T.J.4
  • 15
    • 0028056155 scopus 로고
    • The 1.6 Å structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis
    • Jia, Z., Vandonselaar, M., Hengstenberg, W., Quail, J.W., and Delbaere, L.T.J. 1994a. The 1.6 Å structure of histidine-containing phosphotransfer 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
  • 16
    • 0028440485 scopus 로고
    • Structural comparison of the histidine-containing phosphocarrier protein HPr
    • Jia, Z., Quail, J.W., Delbaere, L.T.J., and Waygood, E.B. 1994b. Structural comparison of the histidine-containing phosphocarrier protein HPr. Biochem. Cell. Biol. 72: 202-217.
    • (1994) Biochem. Cell. Biol. , vol.72 , pp. 202-217
    • Jia, Z.1    Quail, J.W.2    Delbaere, L.T.J.3    Waygood, E.B.4
  • 17
    • 0030760095 scopus 로고    scopus 로고
    • Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis
    • Jones, B.E., Rajagopal, P., and Klevit, R.E. 1997. Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis. Protein Sci. 6: 2107-2119.
    • (1997) Protein Sci. , vol.6 , pp. 2107-2119
    • Jones, B.E.1    Rajagopal, P.2    Klevit, R.E.3
  • 19
    • 0020477463 scopus 로고
    • HPr proteins of different microorganisms studied by hydrogen-1-high resolution of nuclear magnetic resonance: Similarities of structures and mechanisms
    • Kalbitzer, H.R., Hengstenberg, W., Rosch, P., Muss, P., Bernsmann, P., Engelmann, R., Dorschug, M., and Deutscher, J. 1982. HPr proteins of different microorganisms studied by hydrogen-1-high resolution of 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    Rosch, P.3    Muss, P.4    Bernsmann, P.5    Engelmann, R.6    Dorschug, M.7    Deutscher, J.8
  • 20
    • 0026360140 scopus 로고
    • 1H NMR studies on HPr protein from Staphylococcus aureus: Complete sequential assignments and secondary structure
    • 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure. Biochemistry, 30: 11 186-11 192.
    • (1991) Biochemistry , vol.30 , pp. 11186-11192
    • Kalbitzer, H.R.1    Neidig, K.P.2    Hengstenberg, W.3
  • 21
    • 0022925239 scopus 로고
    • 1H NMR studies of histidine-containing protein from Escherichia coli. 2. Leucine resonance assignments by long-range coherence transfers
    • 1H NMR studies of histidine-containing protein from Escherichia coli. 2. Leucine resonance assignments by long-range coherence transfers. Biochemistry, 25: 7770-7773.
    • (1986) Biochemistry , vol.25 , pp. 7770-7773
    • Klevit, R.E.1    Drobny, G.P.2
  • 22
    • 0022925241 scopus 로고
    • 1H NMR studies of histidine-containing protein from Escherichia coli. 3. Secondary and tertiary structure as determined by NMR
    • 1H NMR studies of histidine-containing protein from Escherichia coli. 3. Secondary and tertiary structure as determined by NMR. Biochemistry, 25: 7774-7781.
    • (1986) Biochemistry , vol.25 , pp. 7774-7781
    • Klevit, R.E.1    Waygood, E.B.2
  • 23
    • 0022925244 scopus 로고
    • 1H NMR studies of histidine-containing protein from Escherichia coli. 1. Sequential resonance assignments
    • 1H NMR studies of histidine-containing protein from Escherichia coli. 1. Sequential resonance assignments. Biochemistry, 25: 7760-7769.
    • (1986) Biochemistry , vol.25 , pp. 7760-7769
    • Klevit, R.E.1    Drobny, G.P.2    Waygood, E.B.3
  • 24
    • 0027232148 scopus 로고
    • Involvement of various amino-and carboxyl-terminal residues in the active site of the histidine-containing protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus carnosus: Site directed mutagenesis with the ptsH gene, biochemical characterization and NMR studies of the mutant proteins
    • Kruse, R., Hengstenberg, W., Beneicke, W., and 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-dependent phosphotransferase system of Staphylococcus carnosus: site directed mutagenesis with the ptsH gene, biochemical characterization and NMR studies of the mutant proteins. Protein Eng. 6: 414-423.
    • (1993) Protein Eng. , vol.6 , pp. 414-423
    • Kruse, R.1    Hengstenberg, W.2    Beneicke, W.3    Kalbitzer, H.R.4
  • 25
    • 0000186326 scopus 로고
    • Phosphate bound to a histidine in a protein as an intermediate in a novel phosphotransferase system
    • Kundig, W.S., Ghosh, S., and Roseman, S. 1964. Phosphate bound to a histidine in a protein as an intermediate in a novel phosphotransferase system. Proc. Natl. Acad. Sci. U.S.A. 52: 1067-1074.
    • (1964) Proc. Natl. Acad. Sci. U.S.A. , vol.52 , pp. 1067-1074
    • Kundig, W.S.1    Ghosh, S.2    Roseman, S.3
  • 26
    • 0028774703 scopus 로고
    • Refined structures of the active Ser83 → Cys and impaired Ser46→Asp histidine-containing phosphocarrier proteins
    • Liao, D.-I., and Herzberg, O. 1994. Refined structures of the active Ser83 → Cys and impaired Ser46→Asp histidine-containing phosphocarrier proteins. Structure (London), 2: 203-216.
    • (1994) Structure (London) , vol.2 , pp. 203-216
    • Liao, D.-I.1    Herzberg, O.2
  • 28
    • 0025338715 scopus 로고
    • The bacterial phosphoenolpyruvate:Glycose phosphotransferase system
    • Meadow, N.D., Fox, D.K., and Roseman, S. 1990. The bacterial phosphoenolpyruvate:glycose phosphotransferase system. Annu. Rev. Biochem. 59: 497-542.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 497-542
    • Meadow, N.D.1    Fox, D.K.2    Roseman, S.3
  • 29
    • 9544219681 scopus 로고    scopus 로고
    • Mutation of serine-46 to aspartate in the histidine-containing protein of Escherichia coli mimics the inactivation by phosphorylation of serine-46 in HPrs from Gram-positive bacteria
    • Napper, S., and Anderson, J.W., Georges, F., Quail, J.W., Delbaere, L.T.J., and Waygood, E.B. 1996. Mutation of serine-46 to aspartate in the histidine-containing protein of Escherichia coli mimics the inactivation by phosphorylation of serine-46 in HPrs from Gram-positive bacteria. Biochemistry, 35: 11 260 - 11 267.
    • (1996) Biochemistry , vol.35 , pp. 11260-11267
    • Napper, S.1    Anderson, J.W.2    Georges, F.3    Quail, J.W.4    Delbaere, L.T.J.5    Waygood, E.B.6
  • 31
    • 0029645286 scopus 로고
    • Structural evidence for evolutionary divergence of Mycoplasma from gram-positive bacteria: The histidine-containing phosphocarrier protein structure
    • Pieper, U., Kapadia, G., Zhu, P.-P., Peterkofsky, A., and Herzberg, O. 1995. Structural evidence for evolutionary divergence of Mycoplasma from gram-positive bacteria: the histidine-containing phosphocarrier protein structure. Structure (London), 3: 781-790.
    • (1995) Structure (London) , vol.3 , pp. 781-790
    • Pieper, U.1    Kapadia, G.2    Zhu, P.-P.3    Peterkofsky, A.4    Herzberg, O.5
  • 32
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate:Carbohydrate phosphotransferase system in bacteria
    • Postma, P.W., Lengeler, J.W., and 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
    • 0032584379 scopus 로고    scopus 로고
    • The 2.5 Å resolution structure of the Jel42 Fab fragment/HPr complex
    • Prasad, L., Waygood, E.B., Lee, J.S., and Delbaere, L.T.J. 1998. The 2.5 Å resolution structure of the Jel42 Fab fragment/HPr complex. J. Mol. Biol. 280: 829-845.
    • (1998) J. Mol. Biol. , vol.280 , pp. 829-845
    • Prasad, L.1    Waygood, E.B.2    Lee, J.S.3    Delbaere, L.T.J.4
  • 34
    • 0028818568 scopus 로고
    • Phosphorylation of serine-46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure
    • Pullen, K., Rajagopal, P., Branchini, B.R., Huffine, M.-E., Reizer, J., Saier, M.H., Jr., Scholtz, J.M., and Klevit, R.E. 1995. Phosphorylation of serine-46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure. Protein Sci. 4: 2478-2486.
    • (1995) Protein Sci. , vol.4 , pp. 2478-2486
    • Pullen, K.1    Rajagopal, P.2    Branchini, B.R.3    Huffine, M.-E.4    Reizer, J.5    Saier M.H., Jr.6    Scholtz, J.M.7    Klevit, R.E.8
  • 35
    • 0028589065 scopus 로고
    • Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli
    • Rajagopal, P., Waygood, E.B., and Klevit, R.E. 1994. Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli. Biochemistry, 33: 15 272-15 282.
    • (1994) Biochemistry , vol.33 , pp. 15272-15282
    • Rajagopal, P.1    Waygood, E.B.2    Klevit, R.E.3
  • 36
    • 0027408910 scopus 로고
    • The role of phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system in the regulation of carbon metabolism in gram-positive bacteria
    • Reizer, J., Romano, A.H., and Deutscher, J. 1993. The role of phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system in the regulation of carbon metabolism in gram-positive bacteria. J. Cell. Biochem. 51: 19-24.
    • (1993) J. Cell. Biochem. , vol.51 , pp. 19-24
    • Reizer, J.1    Romano, A.H.2    Deutscher, J.3
  • 37
    • 0019394789 scopus 로고
    • 1H nuclear magnetic resonance studies on the structure and mechanism of the HPr protein of Staphylococcus aureus
    • 1H nuclear magnetic resonance studies on the structure and mechanism of the HPr protein of Staphylococcus aureus. Biochemistry, 20: 1599-1605.
    • (1981) Biochemistry , vol.20 , pp. 1599-1605
    • Rosch, P.1    Kalbitzer, H.R.2    Schmidt-Aderjan, U.3    Hengstenberg, W.4
  • 38
    • 0025906275 scopus 로고
    • Epitope mapping by mutagenesis distinguishes between the two tertiary structures of the histidine-containing protein HPr
    • Sharma, S., Georges, F., Delbaere, L., Lee, J., Klevit, R.E., and Waygood, E.B. 1991. Epitope mapping by mutagenesis distinguishes between the two tertiary structures of the histidine-containing protein HPr. Proc. Natl. Acad. Sci. U.S.A. 88: 4877-4881.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4877-4881
    • Sharma, S.1    Georges, F.2    Delbaere, L.3    Lee, J.4    Klevit, R.E.5    Waygood, E.B.6
  • 39
    • 0027198316 scopus 로고
    • Deamidation of HPr, a phosphocarrier protein of the phosphoenolpyruvate: Sugar phosphotransferase system, involves asparagine 38 (HPr-1) and asparagine 12 (HPr-2) in isoaspartyl acid formation
    • Sharma, S., Hammen, P.K., and Anderson, J.W., Leung, A., Georges, F., Hengstenberg, W., Klevit, R.E., and Waygood, E.B. 1993. Deamidation of HPr, a phosphocarrier protein of the phosphoenolpyruvate: sugar phosphotransferase system, involves asparagine 38 (HPr-1) and asparagine 12 (HPr-2) in isoaspartyl acid formation. J. Biol. Chem. 268: 17 695-17 704.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17695-17704
    • Sharma, S.1    Hammen, P.K.2    Anderson, J.W.3    Leung, A.4    Georges, F.5    Hengstenberg, W.6    Klevit, R.E.7    Waygood, E.B.8
  • 40
  • 42
    • 0026609660 scopus 로고
    • 1H nuclear-magnetic resonance studies of HPr a central component of the phosphoenolpyruvate-dependent phosphotransferase system from Escherichia coli. Assignments of backbone resonances
    • 1H nuclear-magnetic resonance studies of HPr a central component of the phosphoenolpyruvate-dependent phosphotransferase system from Escherichia coli. Assignments of backbone resonances. Eur. J. Biochem. 203: 483-491.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 483-491
    • Van Nuland, N.A.1    Van Dijk, A.A.2    Dijkstra, K.3    Van Hoesel, R.4    Scheek, R.M.5    Robillard, G.T.6
  • 43
    • 0027050395 scopus 로고
    • Determination of the three dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy
    • van Nuland, N.A.J., Grötzinger, J., Dijkstra, K., Scheek, R.M., and Robillard, G.T. 1992b. Determination of the three dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy. Eur. J. Biochem. 210: 881-891.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 881-891
    • Van Nuland, N.A.J.1    Grötzinger, J.2    Dijkstra, K.3    Scheek, R.M.4    Robillard, G.T.5
  • 44
    • 0028360724 scopus 로고
    • The high resolution structure of the histidine containing protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data
    • van Nuland, N.A.J., Hangyi, I.W., van Schaik, R.C., Berendsen, H.J.C., van Gunsteren, W.F., Scheek, R.M., and Robillard, G.T. 1994. The high resolution structure of the histidine containing protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data. J. Mol. Biol. 237: 544-559.
    • (1994) J. Mol. Biol. , vol.237 , pp. 544-559
    • Van Nuland, N.A.J.1    Hangyi, I.W.2    Van Schaik, R.C.3    Berendsen, H.J.C.4    Van Gunsteren, W.F.5    Scheek, R.M.6    Robillard, G.T.7
  • 45
    • 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., Scheek, R.M., and 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    Scheek, R.M.3    Robillard, G.T.4
  • 46
    • 0018965747 scopus 로고
    • Enzyme I of the phosphoenolpyruvate:Sugar phosphotransferase system of Escherichia coli. Purification to homogeneity and some properties
    • Waygood, E.B., and Steeves, T. 1980. Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli. Purification to homogeneity and some properties. Can. J. Biochem. 58: 40-48.
    • (1980) Can. J. Biochem. , vol.58 , pp. 40-48
    • Waygood, E.B.1    Steeves, T.2
  • 47
    • 0022340448 scopus 로고
    • Characterization of phosphorylated histidine-containing protein (HPr) of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system
    • Waygood, E.B., Erickson, E., El-Kabbani, O.A.L., and Delbaere, L.T.J. 1985. Characterization of phosphorylated histidine-containing protein (HPr) of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Biochemistry, 24: 6938-6945.
    • (1985) Biochemistry , vol.24 , pp. 6938-6945
    • Waygood, E.B.1    Erickson, E.2    El-Kabbani, O.A.L.3    Delbaere, L.T.J.4
  • 48
    • 0023922719 scopus 로고
    • Characterization of the 1-phosphohistidinyl residue in the phosphocarrier protein HPr of the phosphoenolpyruvate:Sugar phosphotransferase system of Streptococcus faecalis
    • Waygood, E.B., Pasloske, K., Delbaere, L.T.J., Deutscher, J., and Hengstenberg, W. 1988. Characterization of the 1-phosphohistidinyl residue in the phosphocarrier protein HPr of the phosphoenolpyruvate:sugar phosphotransferase system of Streptococcus faecalis. Biochem. Cell Biol. 66: 76-80.
    • (1988) Biochem. Cell Biol. , vol.66 , pp. 76-80
    • Waygood, E.B.1    Pasloske, K.2    Delbaere, L.T.J.3    Deutscher, J.4    Hengstenberg, W.5
  • 49
    • 0024792738 scopus 로고
    • Common structural changes accompanying the functional inactivation of HPr by seryl phosphorylation or by serine to aspartate substitution
    • Wittekind, M., Reizer, J., Deutscher, J., Saier, M.H., Jr., and Klevit, R.E. 1989a. Common structural changes accompanying the functional inactivation of HPr by seryl phosphorylation or by serine to aspartate substitution. Biochemistry, 28: 9909-9912.
    • (1989) Biochemistry , vol.28 , pp. 9909-9912
    • Wittekind, M.1    Reizer, J.2    Deutscher, J.3    Saier M.H., Jr.4    Klevit, R.E.5
  • 50
    • 0013626025 scopus 로고
    • Study of phosphorylated protein by two-dimensional NMR spectroscopy
    • Chap. 23. Edited by T.E. Hugli. Academic Press, London
    • Wittekind, M., Klevit, R.E., and Waygood, E.B. 1989b. Study of phosphorylated protein by two-dimensional NMR spectroscopy. In Techniques in protein chemistry. Chap. 23. Edited by T.E. Hugli. Academic Press, London. pp. 233-238.
    • (1989) Techniques in Protein Chemistry , pp. 233-238
    • Wittekind, M.1    Klevit, R.E.2    Waygood, E.B.3
  • 51
    • 0025194493 scopus 로고
    • 1H NMR resonance assignments of Bacillus subtilis HPr: Use of spectra obtained from mutants to resolve spectral overlap
    • 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap. Biochemistry, 29: 7191-7200.
    • (1990) Biochemistry , vol.29 , pp. 7191-7200
    • Wittekind, M.1    Reizer, J.2    Klevit, R.E.3
  • 52
    • 0027098199 scopus 로고
    • Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy
    • Wittekind, M., Rajagopal, P., Branchini, B., Reizer, J., Saier, M.H., Jr., and 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.3    Reizer, J.4    Saier M.H., Jr.5    Klevit, R.E.6


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