메뉴 건너뛰기




Volumn 9, Issue 4, 2000, Pages 693-703

15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnosus at high pressure

Author keywords

High pressure; Histidine containing protein; HPr; NMR spectroscopy; Phosphoenolpyruvate dependent phosphotransferase system; PTS

Indexed keywords

HISTIDINE; HISTIDINE CONTAINING PROTEIN; NITROGEN 15; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE; PROTEIN; PROTON; UNCLASSIFIED DRUG; AMIDE; BACTERIAL PROTEIN; NITROGEN; PHOSPHOCARRIER PROTEIN HPR;

EID: 0033624703     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.4.693     Document Type: Article
Times cited : (48)

References (50)
  • 3
    • 0031554921 scopus 로고    scopus 로고
    • Pressure-induced changes in the folded structure of lysozyme
    • Akasaka K, Tezuka T, Yamada H. 1997. Pressure-induced changes in the folded structure of lysozyme. J Mol Biol 277:671-678.
    • (1997) J Mol Biol , vol.277 , pp. 671-678
    • Akasaka, K.1    Tezuka, T.2    Yamada, H.3
  • 6
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen G, Ruben DJ. 1980. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem Phys Lett 69:185-189.
    • (1980) Chem Phys Lett , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 7
    • 0030298077 scopus 로고    scopus 로고
    • On volume changes accompanying conformational transitions of biopolymers
    • Chalikian TV, Breslauer KJ. 1996. On volume changes accompanying conformational transitions of biopolymers. Biopol 39:619-626.
    • (1996) Biopol , vol.39 , pp. 619-626
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 8
    • 0000725483 scopus 로고
    • Thermodynamic fluctuations in protein molecules
    • Cooper A. 1976. Thermodynamic fluctuations in protein molecules. Proc Natl Acad Sci USA 73:2740-2741.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 2740-2741
    • Cooper, A.1
  • 9
    • 0028364161 scopus 로고
    • Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsh gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis
    • Deutscher J, Reizer J, Fischer C, Galinier A, Saier MH, Steinmetz M. 1994. Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsh gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J Bacteriol 176:3336-3344.
    • (1994) J Bacteriol , vol.176 , pp. 3336-3344
    • Deutscher, J.1    Reizer, J.2    Fischer, C.3    Galinier, A.4    Saier, M.H.5    Steinmetz, M.6
  • 10
    • 0028981030 scopus 로고
    • 1H nuclear-magnetic-resonance assignments and structural characterization of a fusion protein of the α-amylase inhibitor tendamistat with the activation domain of the human-immunodeficiency-virus type-1 tat protein
    • 1H nuclear-magnetic-resonance assignments and structural characterization of a fusion protein of the α-amylase inhibitor tendamistat with the activation domain of the human-immunodeficiency-virus type-1 tat protein. J Mol Biol 250:672-688.
    • (1995) J Mol Biol , vol.250 , pp. 672-688
    • Freund, J.1    Vertesy, L.2    Koller, K.P.3    Wolber, V.4    Heintz, D.5    Kalbitzer, H.R.6
  • 11
    • 0022999267 scopus 로고
    • Compressibility-structure relationship of globular proteins
    • Gekko K, Hasegawa J. 1986. Compressibility-structure relationship of globular proteins. Biochemistry 25:6563-6571.
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, J.2
  • 14
    • 0031714901 scopus 로고    scopus 로고
    • Protein structure and dynamics at high pressure
    • Heremans K, Smeller L. 1998. Protein structure and dynamics at high pressure. Biocim Biophys A 1386:353-370.
    • (1998) Biocim Biophys A , vol.1386 , pp. 353-370
    • Heremans, K.1    Smeller, L.2
  • 15
    • 0032574796 scopus 로고    scopus 로고
    • Pressure-dependence of amide hydrogen-deuterium exchange rates for individual sites in T4 lysozyme
    • Hitchens TK, Bryant RG. 1998. Pressure-dependence of amide hydrogen-deuterium exchange rates for individual sites in T4 lysozyme. Biochemistry 37:5878-5887.
    • (1998) Biochemistry , vol.37 , pp. 5878-5887
    • Hitchens, T.K.1    Bryant, R.G.2
  • 16
    • 0032197513 scopus 로고    scopus 로고
    • High pressure NMR study of a small protein, gurmarin
    • Inoue K, Yamada H, Imoto T, Akasaka K. 1998. High pressure NMR study of a small protein, gurmarin. J Biomol NMR 12:535-541.
    • (1998) J Biomol NMR , vol.12 , pp. 535-541
    • Inoue, K.1    Yamada, H.2    Imoto, T.3    Akasaka, K.4
  • 18
    • 0028226052 scopus 로고
    • High-pressure NMR spectroscopy of proteins and membranes
    • Jonas J, Jonas A. 1994. High-pressure NMR spectroscopy of proteins and membranes. Ann Rev Biophys Biom 23:287-318.
    • (1994) Ann Rev Biophys Biom , vol.23 , pp. 287-318
    • Jonas, J.1    Jonas, A.2
  • 19
    • 0030760095 scopus 로고    scopus 로고
    • Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis
    • Jones BE, Rajagopal P, Klevit RE. 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
  • 20
    • 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. Biopol 22:2577-2637.
    • (1983) Biopol , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 21
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced hetero-nuclear single quantum correlation spectroscopy
    • Kay LE, Keifer P, Saarinen T. 1992. Pure absorption gradient enhanced hetero-nuclear single quantum correlation spectroscopy. J Am Chem Soc 114:10663-10665.
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 22
    • 0030787855 scopus 로고    scopus 로고
    • Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: Additivity scheme and implication of protein unfolding at normal and high pressure
    • Kharakoz DP. 1997. Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: Additivity scheme and implication of protein unfolding at normal and high pressure. Biochemistry 36:10276-10285.
    • (1997) Biochemistry , vol.36 , pp. 10276-10285
    • Kharakoz, D.P.1
  • 23
    • 0026785575 scopus 로고
    • Molecular dynamics simulation of solvated protein at high pressure
    • Kitchen DB, Reed LH, Levy RM. 1992. Molecular dynamics simulation of solvated protein at high pressure. Biochemistry 31:10083-10093.
    • (1992) Biochemistry , vol.31 , pp. 10083-10093
    • Kitchen, D.B.1    Reed, L.H.2    Levy, R.M.3
  • 25
    • 0027232148 scopus 로고
    • Involvement of various amino-terminal 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, Kalbitzer HR. 1993. Involvement of various amino-terminal 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
  • 26
    • 0024292355 scopus 로고
    • Effect of hydrostatic pressure on the solvent in crystals of hen egg-white lysozyme
    • Kundrot CE, Richards FM. 1988. Effect of hydrostatic pressure on the solvent in crystals of hen egg-white lysozyme. J Mol Biol 200:401-410.
    • (1988) J Mol Biol , vol.200 , pp. 401-410
    • Kundrot, C.E.1    Richards, F.M.2
  • 28
    • 0028434564 scopus 로고
    • 15N NMR chemical-shifts in proteins and secondary structure
    • 15N NMR chemical-shifts in proteins and secondary structure. J Biomol NMR 4:341-348.
    • (1994) J Biomol NMR , vol.4 , pp. 341-348
    • Le, H.B.1    Oldfield, E.2
  • 29
    • 0032477750 scopus 로고    scopus 로고
    • Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor
    • Li H, Yamada H, Akasaka K. 1998. Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor. Biochemistry 37:1167-1173.
    • (1998) Biochemistry , vol.37 , pp. 1167-1173
    • Li, H.1    Yamada, H.2    Akasaka, K.3
  • 30
    • 0032705720 scopus 로고    scopus 로고
    • Effect of pressure on the tertiary structure and dynamics of folded basic pancreatic trypsin inhibitor
    • Li H, Yamada H, Akasaka K. 1999. Effect of pressure on the tertiary structure and dynamics of folded basic pancreatic trypsin inhibitor. Biophys J 77: 2801-2812.
    • (1999) Biophys J , vol.77 , pp. 2801-2812
    • Li, H.1    Yamada, H.2    Akasaka, K.3
  • 34
    • 0029859688 scopus 로고    scopus 로고
    • Intrinsic compressibility and volume compression in solvated proteins by molecular dynamics simulation at high pressure
    • Paci E, Marchi M. 1996. Intrinsic compressibility and volume compression in solvated proteins by molecular dynamics simulation at high pressure. Proc Natl Acad Sci USA 93:11609-11614.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11609-11614
    • Paci, E.1    Marchi, M.2
  • 35
    • 44049118891 scopus 로고
    • Sensitivity improvement in three-dimensional heteronuclear correlation NMR spectroscopy
    • Palmer AG, Cavanagh J, Byrd RA, Rance M. 1992. Sensitivity improvement in three-dimensional heteronuclear correlation NMR spectroscopy. J Magn Reson 96:416-424.
    • (1992) J Magn Reson , vol.96 , pp. 416-424
    • Palmer, A.G.1    Cavanagh, J.2    Byrd, R.A.3    Rance, M.4
  • 37
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate - Carbohydrate phosphotransferase systems of bacteria
    • Postma PW, Lengeler JW, Jacobson GR. 1993. Phosphoenolpyruvate - carbohydrate phosphotransferase systems of 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
  • 38
    • 0001201618 scopus 로고
    • Structure from NMR and molecular dynamics: Distance restraining inhibits motion in the essential subspace
    • Scheck RM, van Nuland NAJ, de Groot BL, Amadei A. 1995. Structure from NMR and molecular dynamics: Distance restraining inhibits motion in the essential subspace. J Biomol NMR 5:106-111.
    • (1995) J Biomol NMR , vol.5 , pp. 106-111
    • Scheck, R.M.1    Van Nuland, N.A.J.2    De Groot, B.L.3    Amadei, A.4
  • 40
    • 13444269041 scopus 로고
    • Computer-optimized decoupling sheme for wideband applications and low-level operation
    • Shaka AJ, Barker PB, Freeman R. 1985. Computer-optimized decoupling sheme for wideband applications and low-level operation. J Magn Reson 64:541-552.
    • (1985) J Magn Reson , vol.64 , pp. 541-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 41
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor S, Richardson CC. 1985. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc Natl Acad Sci USA 82:1074-1078.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 42
    • 0029963645 scopus 로고    scopus 로고
    • High-resolution triple-resonance NMR spectroscopy of a novel calmodulin peptide complex at kilobar pressures
    • Urbauer JL, Ehrhardt MR, Bieber RJ, Flynn PF, Wand AJ. 1996. High-resolution triple-resonance NMR spectroscopy of a novel calmodulin peptide complex at kilobar pressures. J Am Chem Soc 118:11329-11330.
    • (1996) J Am Chem Soc , vol.118 , pp. 11329-11330
    • Urbauer, J.L.1    Ehrhardt, M.R.2    Bieber, R.J.3    Flynn, P.F.4    Wand, A.J.5
  • 43
    • 0028905499 scopus 로고
    • High-resolution structure of the phosphorylated form of the histidine-containing phospho-carrier protein HPr from Escherichia coli determined by restrained molecular-dynamics from NMR-NOE data
    • van Nuland NAJ, Boelens R, Scheck RM, Robillard GT. 1995. High-resolution structure of the phosphorylated form of the histidine-containing phospho-carrier 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
  • 44
    • 0019318643 scopus 로고
    • 1H NMR at various pressures
    • 1H NMR at various pressures. FEBS Lett 112:280-284.
    • (1980) FEBS Lett , vol.112 , pp. 280-284
    • Wagner, G.1
  • 47
    • 0016056448 scopus 로고
    • Pressure-resisting glass cell for high-pressure, high-resolution NMR measurement
    • Yamada H. 1974. Pressure-resisting glass cell for high-pressure, high-resolution NMR measurement. Rev Sci Instrum 45:640-642.
    • (1974) Rev Sci Instrum , vol.45 , pp. 640-642
    • Yamada, H.1
  • 48
    • 0029143128 scopus 로고
    • Thermodynamics of unfolding of ribonuclease-a under high pressure. A study by proton NMR
    • Yamaguchi T, Yamada H, Akasaka K. 1995. Thermodynamics of unfolding of ribonuclease-A under high pressure. A study by proton NMR. J Mol Biol 250:689-694.
    • (1995) J Mol Biol , vol.250 , pp. 689-694
    • Yamaguchi, T.1    Yamada, H.2    Akasaka, K.3
  • 49
    • 0032559050 scopus 로고    scopus 로고
    • Pressure-denatured state of escherichia coli ribonuclease HI as monitored by Fourier transform infrared and NMR spectroscopy
    • Yamasaki K, Taniguchi Y, Nakano K, Yamasaki T, Kanaya S, Ootabake M. 1998. Pressure-denatured state of Escherichia coli ribonuclease HI as monitored by Fourier transform infrared and NMR spectroscopy. Biochemistry 37:18001-18009.
    • (1998) Biochemistry , vol.37 , pp. 18001-18009
    • Yamasaki, K.1    Taniguchi, Y.2    Nakano, K.3    Yamasaki, T.4    Kanaya, S.5    Ootabake, M.6
  • 50
    • 0026030203 scopus 로고
    • Conformational relaxation of a low-temperature protein as probed by photochemical hole burning. Horseradish peroxidase
    • Zollfrank J, Friedrich J, Vanderkooi JM, Fidy J. 1991. Conformational relaxation of a low-temperature protein as probed by photochemical hole burning. Horseradish peroxidase. Biophys J 59:305-312.
    • (1991) Biophys J , vol.59 , pp. 305-312
    • Zollfrank, J.1    Friedrich, J.2    Vanderkooi, J.M.3    Fidy, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.