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Volumn 5, Issue 2, 1997, Pages 217-225

The structure of an energy-coupling protein from bacteria, IIb(cellobiose), reveals similarity to eukaryotic protein tyrosine phosphatases

Author keywords

carbohydrate transport; cysteine phosphorylation; IIB enzymes; PTS; X ray structure

Indexed keywords

ANIMALIA; BACTERIA (MICROORGANISMS); BOS TAURUS; EUKARYOTA; MAMMALIA;

EID: 0031568849     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00180-9     Document Type: Article
Times cited : (39)

References (47)
  • 1
    • 0028534956 scopus 로고
    • Enzymes II of the phosphoenolpyruvate-dependent phosphotransferase systems: Their structure and function in carbohydrate transport
    • Lengeler, J.W., Jahreis, K. & Wehmeier, U.F. (1994). Enzymes II of the phosphoenolpyruvate-dependent phosphotransferase systems: their structure and function in carbohydrate transport. Biochim. Biophys. Acta 1188, 1-28.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 1-28
    • Lengeler, J.W.1    Jahreis, K.2    Wehmeier, U.F.3
  • 2
    • 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
  • 3
    • 0028104094 scopus 로고
    • The bacterial phosphotransferase system: New frontiers 30 years later
    • Saier Jr., M.H. & Reizer, J. (1994). The bacterial phosphotransferase system: new frontiers 30 years later. Mol. Microbiol. 13, 755-764.
    • (1994) Mol. Microbiol. , vol.13 , pp. 755-764
    • Saier Jr., M.H.1    Reizer, J.2
  • 4
    • 0029616573 scopus 로고
    • Coupling the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli
    • Lux, R., Jahreis, K., Bettenbrock, K., Parkinson, U.S. & Lengeler, J.W. (1995). Coupling the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli. Proc. Natl. Acad. Sci. USA 92, 11583-11587.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11583-11587
    • Lux, R.1    Jahreis, K.2    Bettenbrock, K.3    Parkinson, U.S.4    Lengeler, J.W.5
  • 5
    • 0021088623 scopus 로고
    • Mannitol-specific enzyme II of the bacterial phosphotransferase system III. The nucleotide sequence of the permease gene
    • Lee, C.A. & Saier Jr., M.H. (1983). Mannitol-specific enzyme II of the bacterial phosphotransferase system III. The nucleotide sequence of the permease gene. J. Biol. Chem. 258, 10761-10767.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10761-10767
    • Lee, C.A.1    Saier Jr., M.H.2
  • 6
    • 0025669949 scopus 로고
    • The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus
    • Reizer, J., Reizer, A. & Saier Jr., M.H. (1990). The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus. Res. Microbiol. 141, 1061-1067.
    • (1990) Res. Microbiol. , vol.141 , pp. 1061-1067
    • Reizer, J.1    Reizer, A.2    Saier Jr., M.H.3
  • 7
    • 0027366581 scopus 로고
    • Cloning and sequencing of a cellobiose phosphotransferase system operon from Bacillus stearothermophilus XL-65-6 and functional expression in E. coli
    • Lai, X. & Ingram, L.O. (1993). Cloning and sequencing of a cellobiose phosphotransferase system operon from Bacillus stearothermophilus XL-65-6 and functional expression in E. coli. J. Bacteriol. 175, 6441-6450.
    • (1993) J. Bacteriol. , vol.175 , pp. 6441-6450
    • Lai, X.1    Ingram, L.O.2
  • 9
    • 0030586030 scopus 로고    scopus 로고
    • The first step in sugar transport: Crystal structure of the amino terminal domain of enzyme I of the E. 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 I of the E. 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
  • 10
    • 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
  • 12
    • 0025925213 scopus 로고
    • glc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques
    • glc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques. Biochemistry 30, 10043-10057.
    • (1991) Biochemistry , vol.30 , pp. 10043-10057
    • Pelton, J.G.1    Torchia, D.A.2    Meadow, N.D.3    Wong, C.Y.4    Roseman, S.5
  • 13
    • 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 Jr., M.H., 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
  • 14
    • 0026570487 scopus 로고
    • Low resolution solution structure of the Bacillus subtilis glucose permease IIA domain derived from heteronuclear three-dimensional NMR spectroscopy
    • Fairbrother, W.J., Gippert, G.P., Reizer, J., Saier, M.H.J. & Wright, P.E. (1992). Low resolution solution structure of the Bacillus subtilis glucose permease IIA domain derived from heteronuclear three-dimensional NMR spectroscopy. FEBS Lett. 296, 148-152.
    • (1992) FEBS Lett. , vol.296 , pp. 148-152
    • Fairbrother, W.J.1    Gippert, G.P.2    Reizer, J.3    Saier, M.H.J.4    Wright, P.E.5
  • 16
    • 0029971195 scopus 로고    scopus 로고
    • Structure of the mannose transporter from Escherichia coli at 1.7 Å resolution
    • Nunn, R.S., et al., & Erni, B. (1996). Structure of the mannose transporter from Escherichia coli at 1.7 Å resolution. J. Mol. Biol. 259, 502-511.
    • (1996) J. Mol. Biol. , vol.259 , pp. 502-511
    • Nunn, R.S.1    Erni, B.2
  • 17
    • 0027284018 scopus 로고
    • Backbone assignments and secondary structure of the Escherichia coli enzyme-II mannitol A domain determined by heteronuclear three dimensional spectroscopy
    • Kroon, G.J.A., Grötzinger, J., Dijkstra, K., Scheek, R.M. & Robillard, G.T. (1993). Backbone assignments and secondary structure of the Escherichia coli enzyme-II mannitol A domain determined by heteronuclear three dimensional spectroscopy. Protein Sci. 2, 1331-1341.
    • (1993) Protein Sci. , vol.2 , pp. 1331-1341
    • Kroon, G.J.A.1    Grötzinger, J.2    Dijkstra, K.3    Scheek, R.M.4    Robillard, G.T.5
  • 18
    • 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
  • 19
    • 0029737894 scopus 로고    scopus 로고
    • Solution structure of the IIB domain of the glucose transporter of Escherichia coli
    • Eberstadt, M., Gradnolik, 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    Gradnolik, S.G.2    Gemmecker, G.3    Kessler, H.4    Buhr, A.5    Erni, B.6
  • 20
    • 0029670095 scopus 로고    scopus 로고
    • Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli
    • van Duyne, G.D., Ghosh, G., Maas, W.K. Sigler, P.B. (1996). Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli. J. Mol. Biol. 256, 377-391.
    • (1996) J. Mol. Biol. , vol.256 , pp. 377-391
    • Van Duyne, G.D.1    Ghosh, G.2    Maas, W.K.3    Sigler, P.B.4
  • 21
    • 0017881332 scopus 로고
    • The α helix dipole and the properties of proteins
    • Hol, W.G.J., van Duijnen, P.T. & Berendsen, H.J.C. (1978). The α helix dipole and the properties of proteins. Nature 273, 443-446.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 22
    • 0025741662 scopus 로고
    • Crystal structure of Escherichia coli CheY refined at 1.7 Å resolution
    • Voltz, K. & Matsumura, P. (1991). Crystal structure of Escherichia coli CheY refined at 1.7 Å resolution. J. Biol. Chem. 266, 15511-15519.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15511-15519
    • Voltz, K.1    Matsumura, P.2
  • 23
    • 0028030520 scopus 로고
    • The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase
    • Su, X.D., Taddei, N., Stefani, M., Ramponi, G. & Nordlund, P. (1994). The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase. Nature 370, 575-578.
    • (1994) Nature , vol.370 , pp. 575-578
    • Su, X.D.1    Taddei, N.2    Stefani, M.3    Ramponi, G.4    Nordlund, P.5
  • 24
    • 0027043308 scopus 로고
    • A functional protein hybrid between the glucose transporter and the N-acetylglucosamine transporter of Escherichia coli
    • Hummel, U., Nuoffer, C., Zanolari, B. & Erni, B. (1992). A functional protein hybrid between the glucose transporter and the N-acetylglucosamine transporter of Escherichia coli. Protein Sci. 1, 356-362.
    • (1992) Protein Sci. , vol.1 , pp. 356-362
    • Hummel, U.1    Nuoffer, C.2    Zanolari, B.3    Erni, B.4
  • 25
    • 0027314525 scopus 로고
    • The role of Cys12, Cys17 and Arg18 in the catalytic mechanism of low-Mr cytosolic phosphotyrosine protein phosphatase
    • Cirri, P., et al., & Ramponi, G. (1993). The role of Cys12, Cys17 and Arg18 in the catalytic mechanism of low-Mr cytosolic phosphotyrosine protein phosphatase. Eur. J. Biochem. 214, 647-657.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 647-657
    • Cirri, P.1    Ramponi, G.2
  • 27
    • 85030294694 scopus 로고    scopus 로고
    • cellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli
    • in press
    • cellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. Protein Sci., in press.
    • (1996) Protein Sci.
    • Ab, E.1    Robillard, G.T.2
  • 29
    • 0025327972 scopus 로고
    • Stereochemical course of the reactions catalyzed by the bacterial phosphoenolpyruvate:mannitol phosphotransferase system
    • Mueller, E.G., Khandekar, S.S., Knowles, J.R. & Jacobson, G.R. (1990). Stereochemical course of the reactions catalyzed by the bacterial phosphoenolpyruvate:mannitol phosphotransferase system. Biochemistry 29, 6892-6896.
    • (1990) Biochemistry , vol.29 , pp. 6892-6896
    • Mueller, E.G.1    Khandekar, S.S.2    Knowles, J.R.3    Jacobson, G.R.4
  • 30
    • 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
  • 31
    • 0028670682 scopus 로고
    • 5Arg catalytic motif in phosphoester hydrolysis
    • 5Arg catalytic motif in phosphoester hydrolysis. Biochemistry 33, 15266-15270.
    • (1994) Biochemistry , vol.33 , pp. 15266-15270
    • Zhang, Z.-Y.1    Dixon, J.E.2
  • 32
    • 0028018098 scopus 로고
    • Aspartic-129 is an essential residue in the catalytic mechanism of the low M(r) phosphotyrosine protein phosphatase
    • Taddei, N., et al., & Ramponi, G. (1994). Aspartic-129 is an essential residue in the catalytic mechanism of the low M(r) phosphotyrosine protein phosphatase. FEBS Lett. 350, 328-332.
    • (1994) FEBS Lett. , vol.350 , pp. 328-332
    • Taddei, N.1    Ramponi, G.2
  • 34
    • 0026660314 scopus 로고
    • Site-specific mutagenesis of residues in the Escherichia coli mannitol permease that have been suggested to be important for its phosphorylation and chemoreception functions
    • Weng, Q.-P., Elder, J. & Jacobson, G.R. (1992). Site-specific mutagenesis of residues in the Escherichia coli mannitol permease that have been suggested to be important for its phosphorylation and chemoreception functions. J. Biol. Chem. 267, 19529-19535.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19529-19535
    • Weng, Q.-P.1    Elder, J.2    Jacobson, G.R.3
  • 35
    • 0027991446 scopus 로고
    • The FSSP database of structurally aligned protein fold families
    • Holm, L. & Sander, C. (1994). The FSSP database of structurally aligned protein fold families. Nucl. Acids Res. 22, 3600-3609.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 36
    • 0000319698 scopus 로고
    • Atomic structures and function of periplasmic receptors for active transport and chemotaxis
    • Quiocho, F.A. (1991). Atomic structures and function of periplasmic receptors for active transport and chemotaxis. Curr. Opin. Struct. Biol. 1, 922-933.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 922-933
    • Quiocho, F.A.1
  • 37
    • 0028266197 scopus 로고
    • Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a malto-dependent crystal form
    • Lawson, C.L., et al., & Dijkstra, B.W. (1994). Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a malto-dependent crystal form. J. Mol. Biol. 236, 590-600.
    • (1994) J. Mol. Biol. , vol.236 , pp. 590-600
    • Lawson, C.L.1    Dijkstra, B.W.2
  • 38
    • 0028322353 scopus 로고
    • Crystallization of enzyme IIB of the cellobiose-specific phosphotransferase system of Escherichia coli
    • van Montfort, R.L.M., et al., & Dijkstra, B.W. (1994). Crystallization of enzyme IIB of the cellobiose-specific phosphotransferase system of Escherichia coli. J. Mol. Biol. 239, 588-590.
    • (1994) J. Mol. Biol. , vol.239 , pp. 588-590
    • Van Montfort, R.L.M.1    Dijkstra, B.W.2
  • 39
    • 85027633237 scopus 로고
    • Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography
    • Messerschmidt, A. & Pflugrath, J.W. (1987). Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallography. J. Appl. Cryst. 20, 306-315.
    • (1987) J. Appl. Cryst. , vol.20 , pp. 306-315
    • Messerschmidt, A.1    Pflugrath, J.W.2
  • 40
    • 85046526624 scopus 로고
    • Evaluation of single crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. (1988). Evaluation of single crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Cryst. 21, 916-924.
    • (1988) J. Appl. Cryst. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 41
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4 (1994). The CCP4 Suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 42
    • 0002473587 scopus 로고    scopus 로고
    • Phase combination and cross validation in iterated density modifcation calculations
    • Cowtan, K.D. & Main, P. (1996). Phase combination and cross validation in iterated density modifcation calculations. Acta. Cryst. D 52, 756-764.
    • (1996) Acta. Cryst. D , vol.52 , pp. 756-764
    • Cowtan, K.D.1    Main, P.2
  • 43
    • 0001280470 scopus 로고
    • DEMON/ANGEL: A suite of programs to carry out density modification
    • Vellieux, F.M.D.A.P. (1995). DEMON/ANGEL: a suite of programs to carry out density modification. J. Appl. Cryst. 28, 347-351.
    • (1995) J. Appl. Cryst. , vol.28 , pp. 347-351
    • Vellieux, F.M.D.A.P.1
  • 44
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjelgaard, M. (1991). Improved methods for building 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    Kjelgaard, M.4
  • 45
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 46
    • 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
  • 47
    • 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


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