메뉴 건너뛰기




Volumn 5, Issue 6, 1997, Pages 775-788

The structure of enzyme IIA(lactose) from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system

Author keywords

Enzyme IIA; Helical bundles; Histidine phosphorylation; Modelling; PTS; X ray crystallography

Indexed keywords

BACTERIA (MICROORGANISMS); LACTOCOCCUS LACTIS; TRIXIS;

EID: 0030612122     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00232-3     Document Type: Article
Times cited : (45)

References (72)
  • 1
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma, P.W., Lengeler, J.W. & Jacobson, G.R. (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
  • 2
    • 0027171392 scopus 로고
    • Structure and function of proteins of the phosphotransferase system and of 6-phospho-beta-glycosidases in gram-positive bacteria
    • Hengstenberg, W., et al., & Kalbitzer, H.R. (1993). Structure and function of proteins of the phosphotransferase system and of 6-phospho-beta-glycosidases in gram-positive bacteria. FEMS Microbiol. Rev. 12, 149-163.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 149-163
    • Hengstenberg, W.1    Kalbitzer, H.R.2
  • 3
    • 0025634299 scopus 로고
    • Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis
    • de Vos, W.M., Boerrigter, I., van Rooyen, R.J., Reiche, B. & Hengstenberg, W. (1990). Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis. J. Biol. Chem. 265, 22554-22560.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22554-22560
    • De Vos, W.M.1    Boerrigter, I.2    Van Rooyen, R.J.3    Reiche, B.4    Hengstenberg, W.5
  • 4
    • 0030586030 scopus 로고    scopus 로고
    • The first step in sugar-transport : Crystal-structure of the amino-terminal domain of enzyme-l of the Escherichia coli pep: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr
    • Liao, D.I., Silverton, E., Seok, Y.J., Lee, B.R., Peterkofsky, A. & Davies, D.R. (1996). The first step in sugar-transport : crystal-structure of the amino-terminal domain of enzyme-l of the Escherichia coli pep: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr. Structure 4, 861-872.
    • (1996) Structure , vol.4 , pp. 861-872
    • Liao, D.I.1    Silverton, E.2    Seok, Y.J.3    Lee, B.R.4    Peterkofsky, A.5    Davies, D.R.6
  • 5
    • 0026534155 scopus 로고
    • Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0 a resolution
    • Herzberg, O., Reddy, P., Sutrina, S., Saier, M.H., Jr., Reizer, J. & Kapadia, G. (1992). Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0 A resolution. Proc. Natl. Acad. Sci. 89, 2499-2503.
    • (1992) Proc. Natl. Acad. Sci. , 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
  • 6
    • 0027340388 scopus 로고
    • The 2.0 Å resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination
    • Jia, Z., Quail, J.W., Waygood, E.B. & Delbaere, LT. (1993). The 2.0 Å 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
  • 7
    • 0027458493 scopus 로고
    • Activecentre torsion-angle strain revealed in 1.6A resolution structure of histidine-containing phosphocarrier protein
    • Jia, Z., Vandonselaar, M., Quail, J.W. & Delbaere, LT. (1993). Activecentre torsion-angle strain revealed in 1.6A 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
  • 8
    • 0028056155 scopus 로고
    • The 1.6 a structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis
    • Jia, Z., Vandonselaar, M., Hengstenberg, W., Quail, J.W. & Delbaere, L.T. (1994). The 1.6 A 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
  • 9
    • 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 3, 781-790.
    • (1995) Structure , vol.3 , pp. 781-790
    • Pieper, U.1    Kapadia, G.2    Zhu, P.P.3    Peterkofsky, A.4    Herzberg, O.5
  • 10
    • 0028988431 scopus 로고
    • Investigation of a side-chain-side-chain hydrogen bond by mutagenesis, thermodynamics, and NMR spectroscopy
    • Hammen, P.K., Scholtz, J.M., Anderson, J.W., Waygood, E.B. & Klevit, R.E. (1995). Investigation of a side-chain-side-chain hydrogen bond by mutagenesis, thermodynamics, and NMR spectroscopy. Protein Sci. 4, 936-944.
    • (1995) Protein Sci. , vol.4 , pp. 936-944
    • Hammen, P.K.1    Scholtz, J.M.2    Anderson, J.W.3    Waygood, E.B.4    Klevit, R.E.5
  • 11
    • 0027194655 scopus 로고
    • The solution structure of the histidine-containing protein (HPr) from Staphylococcus aureus as determined by two-dimensional 1 H-NMR spectroscopy
    • Kalbitzer, H.R. & Hengstenberg, W. (1993). The solution structure of the histidine-containing protein (HPr) from Staphylococcus aureus as determined by two-dimensional 1 H-NMR spectroscopy. Eur. J. Biochem. 216, 205-214.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 205-214
    • Kalbitzer, H.R.1    Hengstenberg, W.2
  • 12
    • 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., et al., & 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    Robillard, G.T.2
  • 13
    • 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., Jr. & 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 Jr., M.H.5    Klevit, R.E.6
  • 15
    • 0028587898 scopus 로고
    • Unraveling a bacterial hexose transport pathway
    • Herzberg, O. & 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
  • 16
    • 0026338261 scopus 로고
    • lac of the phosphoenolpyruvate: Sugar phosphotransferase system from Staphylococcus aureus
    • lac of the phosphoenolpyruvate: sugar phosphotransferase system from Staphylococcus aureus. J. Mol. Biol. 222, 857-859.
    • (1991) J. Mol. Biol. , vol.222 , pp. 857-859
    • Celikel, R.1    Reizer, J.2
  • 17
    • 0030485223 scopus 로고    scopus 로고
    • Crystallization and preliminary structural studies of lactose-specific enzyme IIA from Lactococcus lactis
    • Sliz, P., Schröter, K.H., de Vos, W. & Pai, E. (1996). Crystallization and preliminary structural studies of lactose-specific enzyme IIA from Lactococcus lactis. Acta Cryst. D 52, 1199-1201.
    • (1996) Acta Cryst. D , vol.52 , pp. 1199-1201
    • Sliz, P.1    Schröter, K.H.2    De Vos, W.3    Pai, E.4
  • 18
    • 0027284018 scopus 로고
    • Backbone assignments and secondary structure of the Escherichia colienzyme-II mannitol A domain determined by heteronuclear three-dimensional NMR spectroscopy
    • Kroon, G.J., Grotzinger, J., Dijkstra, K., Scheek, R.M. & Robillard, G.T. (1993). Backbone assignments and secondary structure of the Escherichia colienzyme-II mannitol A domain determined by heteronuclear three-dimensional NMR spectroscopy. Protein Sci. 2, 1331-1341.
    • (1993) Protein Sci. , vol.2 , pp. 1331-1341
    • Kroon, G.J.1    Grotzinger, J.2    Dijkstra, K.3    Scheek, R.M.4    Robillard, G.T.5
  • 21
    • 0025940839 scopus 로고
    • Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2 Å resolution
    • Liao, D.I., Kapadia, G., Reddy, P., Saier, M.H., Jr., Reizer, J. & Herzberg, O. (1991). Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2 Å resolution. Biochemistry 30, 9583-9594.
    • (1991) Biochemistry , vol.30 , pp. 9583-9594
    • Liao, D.I.1    Kapadia, G.2    Reddy, P.3    Saier Jr., M.H.4    Reizer, J.5    Herzberg, O.6
  • 22
    • 0029971195 scopus 로고    scopus 로고
    • Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7 Ångstroms resolution
    • Nunn, R.S., et al., & Erni, B. (1996). Structure of the IIA domain of the mannose transporter from Escherichia coli at 1.7 Ångstroms resolution. J. Mol. Biol. 259, 502-511.
    • (1996) J. Mol. Biol. , vol.259 , pp. 502-511
    • Nunn, R.S.1    Erni, B.2
  • 23
    • 0015919159 scopus 로고
    • Sugar transport. IV. Isolation and characterization of the lactose phosphotransferase system in Staphylococcus aureus
    • Simoni, R.D., Nakazawa, T., Hays, J.B. & Roseman, S. (1973). Sugar transport. IV. Isolation and characterization of the lactose phosphotransferase system in Staphylococcus aureus. J. Biol. Chem. 248, 932-940.
    • (1973) J. Biol. Chem. , vol.248 , pp. 932-940
    • Simoni, R.D.1    Nakazawa, T.2    Hays, J.B.3    Roseman, S.4
  • 26
    • 0029737894 scopus 로고    scopus 로고
    • Solution structure of the IIB domain of the glucose transporter of Escherichia coli
    • Eberstadt, M., Grdadolnik, S.G., Gemmecker, G., Kessler, H., Buhr, A. & Erni, B. (1996). Solution structure of the IIB domain of the glucose transporter of Escherichia coli. Biochemistry 35, 11286-11292.
    • (1996) Biochemistry , vol.35 , pp. 11286-11292
    • Eberstadt, M.1    Grdadolnik, S.G.2    Gemmecker, G.3    Kessler, H.4    Buhr, A.5    Erni, B.6
  • 27
    • 0031568849 scopus 로고    scopus 로고
    • cellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases
    • cellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. Structure 5, 217-225.
    • (1997) Structure , vol.5 , pp. 217-225
    • Van Monfort, R.L.1    Dijkstra, B.W.2
  • 28
    • 0031042397 scopus 로고    scopus 로고
    • cellbiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli
    • cellbiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. Protein Sci. 6, 304-314.
    • (1997) Protein Sci. , vol.6 , pp. 304-314
    • Eiso, A.B.1    Robillard, G.T.2
  • 29
    • 0015919110 scopus 로고
    • Sugar transport. V. A trimeric lactose-specific phosphocarrier protein of the Staphylococcus aureus phosphotransferase system
    • Hays, J.B., Simoni, R.D. & Roseman, S. (1973). Sugar transport. V. A trimeric lactose-specific phosphocarrier protein of the Staphylococcus aureus phosphotransferase system. J. Biol. Chem. 248, 941-956.
    • (1973) J. Biol. Chem. , vol.248 , pp. 941-956
    • Hays, J.B.1    Simoni, R.D.2    Roseman, S.3
  • 30
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, 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
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 32
    • 0024279567 scopus 로고
    • One type of gamma-turn, rather than the other gives rise to chain-reversal in proteins
    • Milner-White, E., Ross, B.M., Ismail, R., Belhadj- Mostefa, K. & Poet, R. (1988). One type of gamma-turn, rather than the other gives rise to chain-reversal in proteins. J. Mol. Biol. 204, 777-782.
    • (1988) J. Mol. Biol. , vol.204 , pp. 777-782
    • Milner-White, E.1    Ross, B.M.2    Ismail, R.3    Belhadj- Mostefa, K.4    Poet, R.5
  • 34
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B. & Sander, C. (1993). Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 35
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B. & Sander, C. (1994). Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19, 55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 36
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P.Y. & Fasman, G.D. (1974). Prediction of protein conformation. Biochemistry 13, 222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 37
    • 0017709445 scopus 로고
    • Beta-turns in proteins
    • Chou, P.Y. & Fasman, G.D. (1977). Beta-turns in proteins. J. Mol. Biol. 115, 135-175.
    • (1977) J. Mol. Biol. , vol.115 , pp. 135-175
    • Chou, P.Y.1    Fasman, G.D.2
  • 39
    • 0027787871 scopus 로고
    • The crystal structure of lysin, a fertilization protein
    • Shaw, A., McRee, D.E., Vacquier, V.D. & Stout, C.D. (1993). The crystal structure of lysin, a fertilization protein. Science 262, 1864-1867.
    • (1993) Science , vol.262 , pp. 1864-1867
    • Shaw, A.1    McRee, D.E.2    Vacquier, V.D.3    Stout, C.D.4
  • 40
    • 0027416662 scopus 로고
    • Crystal structure of a synthetic triple-stranded alpha-helical bundle
    • Lovejoy, B., Choe, S., Cascio, D., McRorie, D.K., DeGrado, W.F. & Eisenberg, D. (1993). Crystal structure of a synthetic triple-stranded alpha-helical bundle. Science 259, 1288-1293.
    • (1993) Science , vol.259 , pp. 1288-1293
    • Lovejoy, B.1    Choe, S.2    Cascio, D.3    McRorie, D.K.4    DeGrado, W.F.5    Eisenberg, D.6
  • 42
    • 0029958604 scopus 로고    scopus 로고
    • A test of the jigsaw puzzle model for protein folding by multiple methionine substitutions within the core of T4 lysozyme
    • Gassner, N.C., Baase, W.A. & Matthews, B.W. (1996). A test of the jigsaw puzzle model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. Proc. Natl. Acad. Sci. USA 93, 12155-12158.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12155-12158
    • Gassner, N.C.1    Baase, W.A.2    Matthews, B.W.3
  • 43
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas, A. (1996). Coiled coils: new structures and new functions. Trends Biochem. Sci. 21, 375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 44
    • 0017729207 scopus 로고
    • Enzymology of carbohydrate transport in bacteria
    • Hengstenberg, W. (1977). Enzymology of carbohydrate transport in bacteria. Curr. Topics in Microbiol. Immunol. 77, 97-1 26.
    • (1977) Curr. Topics in Microbiol. Immunol. , vol.77 , pp. 97-126
    • Hengstenberg, W.1
  • 45
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in proteins
    • Glusker, J.P. (1991). Structural aspects of metal liganding to functional groups in proteins. Adv. Protein Chem. 42, 1-76.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 1-76
    • Glusker, J.P.1
  • 46
    • 12644295057 scopus 로고    scopus 로고
    • Crystal structure of dUTP pyrophosphatase from feline immunodeficiency virus
    • Prasad, G.S., et al., & Stout, C.D. (1996). Crystal structure of dUTP pyrophosphatase from feline immunodeficiency virus. Protein Sci. 5, 2429-2437.
    • (1996) Protein Sci. , vol.5 , pp. 2429-2437
    • Prasad, G.S.1    Stout, C.D.2
  • 47
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T. & Chothia, C. (1995). SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 48
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein, F.C., et al., & Tasumi, M. (1977). The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Tasumi, M.2
  • 49
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 50
    • 0026315513 scopus 로고
    • Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • Milburn, M.V., et al., & Kim, S.H. (1991). Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science 254, 1342-1347.
    • (1991) Science , vol.254 , pp. 1342-1347
    • Milburn, M.V.1    Kim, S.H.2
  • 51
    • 0025922235 scopus 로고
    • lac of the Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: Sitespecific mutagenesis of histidine residues, biochemical characterization and 1H-NMR studies
    • lac of the Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: sitespecific mutagenesis of histidine residues, biochemical characterization and 1H-NMR studies. Protein Eng. 4, 469-473.
    • (1991) Protein Eng. , vol.4 , pp. 469-473
    • Finkeldei, U.1    Kalbitzer, H.R.2    Eisermann, R.3    Stewart, G.C.4    Hengstenberg, W.5
  • 53
    • 0027050395 scopus 로고
    • Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coil using multidimensional NMR spectroscopy
    • van Nuland, N.A., Grotzinger, J., Dijkstra, K., Scheek, R.M. & Robillard, G.T. (1992). Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coil using multidimensional NMR spectroscopy. Eur. J. Biochem. 210, 881-891.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 881-891
    • Van Nuland, N.A.1    Grotzinger, J.2    Dijkstra, K.3    Scheek, R.M.4    Robillard, G.T.5
  • 54
    • 0026483795 scopus 로고
    • An atomic model for protein-protein phosphoryl group transfer
    • Herzberg, O. (1992). An atomic model for protein-protein phosphoryl group transfer. J. Biol. Chem. 267, 24819-24823.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24819-24823
    • Herzberg, O.1
  • 55
    • 0029822166 scopus 로고    scopus 로고
    • Main-chain complementarity in protein-protein recognition
    • Vakser, I.A. (1996). Main-chain complementarity in protein-protein recognition. Protein Eng. 9, 741-744.
    • (1996) Protein Eng. , vol.9 , pp. 741-744
    • Vakser, I.A.1
  • 56
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin, J. & Chothia, C. (1990). The structure of protein-protein recognition sites. J. Biol. Chem. 265, 16027-16030.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 58
    • 0028338720 scopus 로고
    • Inhibition of the phosphoenolpyruvate: Lactose phosphotransferase system and activation of a cytoplasmic sugar-phosphate phosphatase in Lactococcus lactis by ATP-dependent metabolite- Activated phosphorylation of serine 46 in the phosphocarrier protein HPr
    • Ye, J.J., Reizer, J., Cui, X. & Saier, M.H., Jr. (1994). Inhibition of the phosphoenolpyruvate: lactose phosphotransferase system and activation of a cytoplasmic sugar-phosphate phosphatase in Lactococcus lactis by ATP-dependent metabolite- activated phosphorylation of serine 46 in the phosphocarrier protein HPr. J. Biol. Chem. 269, 11837-11844.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11837-11844
    • Ye, J.J.1    Reizer, J.2    Cui, X.3    Saier Jr., M.H.4
  • 59
    • 9544219681 scopus 로고    scopus 로고
    • Mutation of serine-46 to aspartate in the histidine-containing protein of Escherichia coil mimics the inactivation by phosphorylation of serine-46 in HPrs from gram-positive bacteria
    • Napper, S., Anderson, J.W., Georges, F., Quail, J.W., Delbaere, L.T. & Waygood, E.B. (1996). Mutation of serine-46 to aspartate in the histidine-containing protein of Escherichia coil 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.5    Waygood, E.B.6
  • 60
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer, L., Isaacs, N. & Bailey, S., eds, SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend. (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 61
    • 80055004570 scopus 로고
    • Generalized method of determining heavy-atom positions using difference Patterson function
    • Terwilliger, T.C., Kim, S.-H. & Eisenberg, G. (1987). Generalized method of determining heavy-atom positions using difference Patterson function. Acta Cryst. A 43, 1-5.
    • (1987) Acta Cryst. A , vol.43 , pp. 1-5
    • Terwilliger, T.C.1    Kim, S.-H.2    Eisenberg, G.3
  • 63
    • 0002700643 scopus 로고
    • Halloween ... Masks and Bones
    • Bailey, S., Hubbard, R. & Waller, D., eds, SERC Daresbury Laboratory, Warrington, UK
    • Kleywegt, G.J. & Jones, T.A. (1994). Halloween .... Masks and Bones. In From First Map to Final Model. (Bailey, S., Hubbard, R. & Waller, D., eds), pp. 59-66, SERC Daresbury Laboratory, Warrington, UK.
    • (1994) From First Map to Final Model , pp. 59-66
    • Kleywegt, G.J.1    Jones, T.A.2
  • 64
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron-density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for the building of protein models in electron-density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 66
    • 0002065270 scopus 로고    scopus 로고
    • Making the most of your search model
    • Kleywegt, G.J. (1996). Making the most of your search model. ESF/CCP4 Newsletter. 32, 32-36.
    • (1996) ESF/CCP4 Newsletter , vol.32 , pp. 32-36
    • Kleywegt, G.J.1
  • 67
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF a program to identify and analyze structural motifs in proteins
    • Hutchinson, E.G. & Thornton, J.M. (1996). PROMOTIF a program to identify and analyze structural motifs in proteins. Protein Sci. 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 69
    • 0003916136 scopus 로고
    • Columbia University, NY, USA
    • Nicholls, A.J. (1993). GRASP Manual. Columbia University, NY, USA.
    • (1993) GRASP Manual
    • Nicholls, A.J.1
  • 70
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 72
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representation of macromolecules
    • Evans, S.V. (1993). SETOR: hardware-lighted three-dimensional solid model representation of macromolecules. J. Mol. Graph. 11, 134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.