메뉴 건너뛰기




Volumn 46, Issue 43, 2007, Pages 12314-12326

Effects of histidine protonation and phosphorylation on histidine-containing phosphocarrier protein structure, dynamics, and physicochemical properties

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL RIGIDITY; PHOSPHOTRANSFER REACTIONS; PHYSICOCHEMICAL PROPERTIES;

EID: 35648949313     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701228g     Document Type: Article
Times cited : (8)

References (50)
  • 1
    • 0000186326 scopus 로고
    • Phosphate Bound to Histidine in a Protein as an Intermediate in a Novel Phospho-Transferase System
    • Kundig, W., Ghosh, S., and Roseman, S. (1964) Phosphate Bound to Histidine in a Protein as an Intermediate in a Novel Phospho-Transferase 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.1    Ghosh, S.2    Roseman, S.3
  • 2
    • 0036693775 scopus 로고    scopus 로고
    • Global control of sugar metabolism: A Gram-positive solution
    • Titgemeyer, F., and Hillen, W. (2002) Global control of sugar metabolism: A Gram-positive solution, Antonie Van Leeuwenhoek 82, 59-71.
    • (2002) Antonie Van Leeuwenhoek , vol.82 , pp. 59-71
    • Titgemeyer, F.1    Hillen, W.2
  • 3
    • 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 Jr., M.H.2
  • 5
    • 0032453554 scopus 로고    scopus 로고
    • The structure and function of HPr
    • Waygood, E. B. (1998) The structure and function of HPr, Biochem. Cell Biol. 76, 359-367.
    • (1998) Biochem. Cell Biol , vol.76 , pp. 359-367
    • Waygood, E.B.1
  • 6
    • 0031774448 scopus 로고    scopus 로고
    • Coupling physiology and gene regulation in bacteria: The phosphotransferase sugar uptake system delivers the signals
    • Stulke, J., and Hillen, W. (1998) Coupling physiology and gene regulation in bacteria: The phosphotransferase sugar uptake system delivers the signals, Naturwissenschaften 85, 583-592.
    • (1998) Naturwissenschaften , vol.85 , pp. 583-592
    • Stulke, J.1    Hillen, W.2
  • 7
    • 0035702148 scopus 로고    scopus 로고
    • Bacterial phosphotransferase system (PTS) in carbohydrate uptake and control of carbon metabolism
    • Kotrba, P., Inui, M., and Yukawa, H. (2001) Bacterial phosphotransferase system (PTS) in carbohydrate uptake and control of carbon metabolism, J. Biosci. Bioeng. 92, 502-517.
    • (2001) J. Biosci. Bioeng , vol.92 , pp. 502-517
    • Kotrba, P.1    Inui, M.2    Yukawa, H.3
  • 8
    • 0031808469 scopus 로고    scopus 로고
    • PRD: A protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria
    • Stulke, J., Arnaud, M., Rapoport, G., and Martin-Verstraete, I. (1998) PRD: A protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria, Mol. Microbiol. 28, 865-874.
    • (1998) Mol. Microbiol. 28 , pp. 865-874
    • Stulke, J.1    Arnaud, M.2    Rapoport, G.3    Martin-Verstraete, I.4
  • 9
    • 0028360724 scopus 로고
    • The high-resolution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data
    • van Nuland, N. A., Hangyi, I. W., van Schaik, R. C., Berendsen, H. J., van Gunsteren, W. F., Scheek, R. M., and Robillard, G. T. (1994) The high-resolution structure of the histidine-containing phosphocarrier 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.1    Hangyi, I.W.2    van Schaik, R.C.3    Berendsen, H.J.4    van Gunsteren, W.F.5    Scheek, R.M.6    Robillard, G.T.7
  • 10
    • 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., 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.1    Boelens, R.2    Scheek, R.M.3    Robillard, G.T.4
  • 11
    • 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. (1994) 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.5
  • 13
    • 0034829186 scopus 로고    scopus 로고
    • Three-dimensional structure of the histidine-containing phosphocarrier protein (HPr) from Enterococcus faecalis in solution
    • Maurer, T., Doker, R., Gorler, A., Hengstenberg, W., and Kalbitzer, H. R. (2001) Three-dimensional structure of the histidine-containing phosphocarrier protein (HPr) from Enterococcus faecalis in solution, Eur. J. Biochem. 268, 635-644.
    • (2001) Eur. J. Biochem , vol.268 , pp. 635-644
    • Maurer, T.1    Doker, R.2    Gorler, A.3    Hengstenberg, W.4    Kalbitzer, H.R.5
  • 14
    • 0026534155 scopus 로고
    • Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-Å resolution
    • Herzberg, O., Reddy, P., Sutrina, S., Saier, M. H., Jr., 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    Sutrina, S.3    Saier Jr., M.H.4    Reizer, J.5    Kapadia, G.6
  • 15
    • 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
  • 17
    • 11244296117 scopus 로고    scopus 로고
    • Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus
    • Moglich, A., Koch, B., Gronwald, W., Hengstenberg, W., Brunner, E., and Kalbitzer, H. R. (2004) Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus, Eur. J. Biochem. 271, 4815-4824.
    • (2004) Eur. J. Biochem , vol.271 , pp. 4815-4824
    • Moglich, A.1    Koch, B.2    Gronwald, W.3    Hengstenberg, W.4    Brunner, E.5    Kalbitzer, H.R.6
  • 18
    • 4344634292 scopus 로고    scopus 로고
    • High-resolution structure of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus aureus and characterization of its interaction with the bifunctional HPr kinase/phosphorylase
    • Maurer, T., Meier, S., Kachel, N., Munte, C. E., Hasenbein, S., Koch, B., Hengstenberg, W., and Kalbitzer, H. R. (2004) High-resolution structure of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus aureus and characterization of its interaction with the bifunctional HPr kinase/phosphorylase, J. Bacteriol. 186, 5906-5918.
    • (2004) J. Bacteriol , vol.186 , pp. 5906-5918
    • Maurer, T.1    Meier, S.2    Kachel, N.3    Munte, C.E.4    Hasenbein, S.5    Koch, B.6    Hengstenberg, W.7    Kalbitzer, H.R.8
  • 20
    • 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, 417-423.
    • (1993) Protein Eng , vol.6 , pp. 417-423
    • Kruse, R.1    Hengstenberg, W.2    Beneicke, W.3    Kalbitzer, H.R.4
  • 21
    • 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, J. W., and Delbaere, L. T. (1993) Active-centre torsion-angle strain revealed in 1.6 Å-resolution structure of histidine-containing phosphocarrier protein, Nature 361, 94-97.
    • (1993) Nature , vol.361 , pp. 94-97
    • Jia, Z.1    Vandonselaar, M.2    Quail, J.W.3    Delbaere, L.T.4
  • 22
    • 0000000699 scopus 로고    scopus 로고
    • Electrostatic models for computing protonation and redox equilibria in proteins
    • Ullmann, G. M., and Knapp, E. W. (1999) Electrostatic models for computing protonation and redox equilibria in proteins, Eur. Biophys. J. 28, 533-551.
    • (1999) Eur. Biophys. J , vol.28 , pp. 533-551
    • Ullmann, G.M.1    Knapp, E.W.2
  • 24
    • 33644753023 scopus 로고    scopus 로고
    • AMBER force-field parameters for phosphorylated amino acids in different protonation states: Phosphoserine, phosphothreonine, phosphotyrosine, and phosphohistidine
    • Homeyer, N., Horn, A. H. C., Lanig, H., and Sticht, H. (2006) AMBER force-field parameters for phosphorylated amino acids in different protonation states: Phosphoserine, phosphothreonine, phosphotyrosine, and phosphohistidine, J. Mol. Model. 12, 281-289.
    • (2006) J. Mol. Model , vol.12 , pp. 281-289
    • Homeyer, N.1    Horn, A.H.C.2    Lanig, H.3    Sticht, H.4
  • 26
    • 0026612756 scopus 로고
    • Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin
    • Bashford, D., and Gerwert, K. (1992) Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin, J. Mol. Biol. 224, 473-486.
    • (1992) J. Mol. Biol , vol.224 , pp. 473-486
    • Bashford, D.1    Gerwert, K.2
  • 27
  • 28
    • 0015520587 scopus 로고
    • Interpretation of protein titration curves. Application to lysozyme
    • Tanford, C., and Roxby, R. (1972) Interpretation of protein titration curves. Application to lysozyme, Biochemistry 11, 2192-2198.
    • (1972) Biochemistry , vol.11 , pp. 2192-2198
    • Tanford, C.1    Roxby, R.2
  • 33
    • 0032922174 scopus 로고    scopus 로고
    • Cheatham, T. E., III, Cieplak, P., and Kollman, P. A. (1999) A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat, J. Biomol. Struct. Dyn. 16, 845-862.
    • Cheatham, T. E., III, Cieplak, P., and Kollman, P. A. (1999) A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat, J. Biomol. Struct. Dyn. 16, 845-862.
  • 34
    • 33947581228 scopus 로고    scopus 로고
    • Effect of HPr phosphorylation on structure, dynamics, and interactions in the course of transcriptional control
    • Homeyer, N., Essigke, T., Meiselbach, H., Ullmann, G. M., and Sticht, H. (2006) Effect of HPr phosphorylation on structure, dynamics, and interactions in the course of transcriptional control, J. Mol. Model. 13, 431-444.
    • (2006) J. Mol. Model , vol.13 , pp. 431-444
    • Homeyer, N.1    Essigke, T.2    Meiselbach, H.3    Ullmann, G.M.4    Sticht, H.5
  • 36
    • 0004283184 scopus 로고
    • Yale University Press, New Haven, CT
    • Brünger, A. T. (1992) X-PLOR, Yale University Press, New Haven, CT.
    • (1992) X-PLOR
    • Brünger, A.T.1
  • 37
    • 35649012321 scopus 로고
    • St. Louis, MO
    • Tripos (1991-2002) SYBYL, St. Louis, MO.
    • (1991) SYBYL
    • Tripos1
  • 38
    • 0032520183 scopus 로고    scopus 로고
    • Structural studies of histidine-containing phosphocarrier protein from Enterococcus faecalis
    • Hahmann, M., Maurer, T., Lorenz, M., Hengstenberg, W., Glaser, S., and Kalbitzer, H. R. (1998) Structural studies of histidine-containing phosphocarrier protein from Enterococcus faecalis, Eur. J. Biochem. 252, 51-58.
    • (1998) Eur. J. Biochem , vol.252 , pp. 51-58
    • Hahmann, M.1    Maurer, T.2    Lorenz, M.3    Hengstenberg, W.4    Glaser, S.5    Kalbitzer, H.R.6
  • 39
    • 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, 15271-15282.
    • (1994) Biochemistry , vol.33 , pp. 15271-15282
    • Rajagopal, P.1    Waygood, E.B.2    Klevit, R.E.3
  • 40
    • 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., 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 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
  • 41
    • 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, 12325-12333.
    • (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
  • 42
    • 0018118592 scopus 로고
    • Carbon-13 NMR Chemical Shifts of the Common Amino Acid Residues Measured in Aqueous Solutions of the Linear Tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • Richarz, R., and Wüthrich, K. (1978) Carbon-13 NMR Chemical Shifts of the Common Amino Acid Residues Measured in Aqueous Solutions of the Linear Tetrapeptides H-Gly-Gly-X-L-Ala-OH, Biopolymers 17, 2133-2141.
    • (1978) Biopolymers , vol.17 , pp. 2133-2141
    • Richarz, R.1    Wüthrich, K.2
  • 43
    • 0037421933 scopus 로고    scopus 로고
    • Relations between Protonation Constants and Titration Curves in Polyprotic Acids: A Critical View
    • Ullmann, G. M. (2003) Relations between Protonation Constants and Titration Curves in Polyprotic Acids: A Critical View, J. Phys. Chem. B 107, 1263-1271.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 1263-1271
    • Ullmann, G.M.1
  • 44
    • 33745099338 scopus 로고    scopus 로고
    • Theoretical investigation of the behavior of titratable groups in proteins
    • Klingen, A. R., Bombarda, E., and Ullmann, G. M. (2006) Theoretical investigation of the behavior of titratable groups in proteins, Photochem. Photobiol. Sci. 5, 588-596.
    • (2006) Photochem. Photobiol. Sci , vol.5 , pp. 588-596
    • Klingen, A.R.1    Bombarda, E.2    Ullmann, G.M.3
  • 45
    • 0032939176 scopus 로고    scopus 로고
    • Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr
    • Garrett, D. S., Seok, Y. J., Peterkofsky, A., Gronenborn, A. M., and Clore, G. M. (1999) Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr, Nat. Struct. Biol. 6, 166-173.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 166-173
    • Garrett, D.S.1    Seok, Y.J.2    Peterkofsky, A.3    Gronenborn, A.M.4    Clore, G.M.5
  • 46
    • 0036829797 scopus 로고    scopus 로고
    • Solution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Escherichia coli phosphotransferase system
    • Cornilescu, G., Lee, B. R., Cornilescu, C. C., Wang, G., Peterkofsky, A., and Clore, G. M. (2002) Solution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Escherichia coli phosphotransferase system, J. Biol. Chem. 277, 42289-42298.
    • (2002) J. Biol. Chem , vol.277 , pp. 42289-42298
    • Cornilescu, G.1    Lee, B.R.2    Cornilescu, C.C.3    Wang, G.4    Peterkofsky, A.5    Clore, G.M.6
  • 47
    • 0034329415 scopus 로고    scopus 로고
    • Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIA(glucose) of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system
    • Wang, G., Louis, J. M., Sondej, M., Seok, Y. J., Peterkofsky, A., and Clore, G. M. (2000) Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIA(glucose) of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system, EMBO J. 19, 5635-5649.
    • (2000) EMBO J , vol.19 , pp. 5635-5649
    • Wang, G.1    Louis, J.M.2    Sondej, M.3    Seok, Y.J.4    Peterkofsky, A.5    Clore, G.M.6
  • 48
    • 20144384787 scopus 로고    scopus 로고
    • Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system
    • Williams, D. C., Jr., Cai, M., Suh, J. Y., Peterkofsky, A., and Clore, G. M. (2005) Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system, J. Biol. Chem. 280, 20775-20784.
    • (2005) J. Biol. Chem , vol.280 , pp. 20775-20784
    • Williams Jr., D.C.1    Cai, M.2    Suh, J.Y.3    Peterkofsky, A.4    Clore, G.M.5
  • 49
    • 4544356004 scopus 로고    scopus 로고
    • Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P
    • Schumacher, M. A., Allen, G. S., Diel, M., Seidel, G., Hillen, W., and Brennan, R. G. (2004) Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P, Cell 118, 731-741.
    • (2004) Cell , vol.118 , pp. 731-741
    • Schumacher, M.A.1    Allen, G.S.2    Diel, M.3    Seidel, G.4    Hillen, W.5    Brennan, R.G.6
  • 50
    • 34147143867 scopus 로고    scopus 로고
    • Structural Mechanism for the Fine-tuning of CcpA Function by The Small Molecule Effectors Glucose 6-Phosphate and Fructose 1,6-Bisphosphate
    • Schumacher, M. A., Seidel, G., Hillen, W., and Brennan, R. G. (2007) Structural Mechanism for the Fine-tuning of CcpA Function by The Small Molecule Effectors Glucose 6-Phosphate and Fructose 1,6-Bisphosphate, J. Mol. Biol. 368, 1042-1050.
    • (2007) J. Mol. Biol , vol.368 , pp. 1042-1050
    • Schumacher, M.A.1    Seidel, G.2    Hillen, W.3    Brennan, R.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.