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Volumn 287, Issue 5, 1999, Pages 845-851

The 5 Å projection structure of the transmembrane domain of the mannitol transporter enzyme II

Author keywords

2 dimensional crystallisation; Electron crystallography; Enzyme IIC mannitol; Membrane protein; PTS

Indexed keywords

CARRIER PROTEIN; DIMER; MANNITOL; MEMBRANE PROTEIN; MONOMER; PHOSPHOENOLPYRUVATE MANNITOL PHOSPHOTRANSFERASE; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE; PHOSPHOENOLPYRUVATE-MANNITOL PHOSPHOTRANSFERASE;

EID: 0033574275     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2650     Document Type: Article
Times cited : (43)

References (36)
  • 1
    • 0021582830 scopus 로고
    • Measurement and evaluation of electron diffraction patterns from two-dimensional crystals
    • Baldwin J. M., Henderson R. Measurement and evaluation of electron diffraction patterns from two-dimensional crystals. Ultramicroscopy. 14:1984;319-336.
    • (1984) Ultramicroscopy , vol.14 , pp. 319-336
    • Baldwin, J.M.1    Henderson, R.2
  • 2
    • 0029846910 scopus 로고    scopus 로고
    • Relation between the oligomerization state and the transport and phosphorylation function of the Escherichia coli mannitol transport protein: Interaction between mannitol-specific enzyme II monomers studied by complementation of inactive site-directed mutants
    • Boer H., ten Hoeve-Duurkens R. H., Robillard G. T. Relation between the oligomerization state and the transport and phosphorylation function of the Escherichia coli mannitol transport protein: interaction between mannitol-specific enzyme II monomers studied by complementation of inactive site-directed mutants. Biochemistry. 35:1996;12901-12908.
    • (1996) Biochemistry , vol.35 , pp. 12901-12908
    • Boer, H.1    Ten Hoeve-Duurkens, R.H.2    Robillard, G.T.3
  • 4
    • 0027207386 scopus 로고
    • Membrane topology of the glucose transporter of Escherichia coli
    • Buhr A., Erni B. Membrane topology of the glucose transporter of Escherichia coli. J. Biol. Chem. 268:1993;11599-11603.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11599-11603
    • Buhr, A.1    Erni, B.2
  • 6
    • 0030015012 scopus 로고    scopus 로고
    • A fluorescence study of single tryptophan-containing mutants of enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent mannitol transport system
    • Dijkstra D. S., Broos J., Lolkema J. S., Enequist H., Minke W., Robillard G. T. A fluorescence study of single tryptophan-containing mutants of enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent mannitol transport system. Biochemistry. 35:1996;6628-6634.
    • (1996) Biochemistry , vol.35 , pp. 6628-6634
    • Dijkstra, D.S.1    Broos, J.2    Lolkema, J.S.3    Enequist, H.4    Minke, W.5    Robillard, G.T.6
  • 7
    • 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. Solution structure of the IIB domain of the glucose transporter of Escherichia coli. Biochemistry. 35:1996;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
  • 8
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J. M., Ceska T. A., Zemlin F., Beckmann E., Downing K. H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:1990;899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 9
    • 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 L. T. The 2.0 Å resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination. J. Biol. Chem. 268:1993;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
  • 10
    • 0024518066 scopus 로고
    • Evidence for two distinct conformations of the Escherichia coli mannitol permease that are important for its transport and phosphorylation functions
    • Khandekar S. S., Jacobson G. R. Evidence for two distinct conformations of the Escherichia coli mannitol permease that are important for its transport and phosphorylation functions. J. Cell Biochem. 39:1989;207-216.
    • (1989) J. Cell Biochem. , vol.39 , pp. 207-216
    • Khandekar, S.S.1    Jacobson, G.R.2
  • 11
    • 0021088623 scopus 로고
    • Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. The nucleotide sequence of the permease gene
    • Lee C. A., Saier M. H. Jr. Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. The nucleotide sequence of the permease gene. J. Biol. Chem. 258:1983;10761-10767.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10761-10767
    • Lee, C.A.1    Saier M.H., Jr.2
  • 12
    • 0024679269 scopus 로고
    • Molecular mechanisms of bacterial chemotaxis towards PTS-carbohydrates
    • Lengeler J. W., Vogler A. P. Molecular mechanisms of bacterial chemotaxis towards PTS-carbohydrates. FEMS Microbiol. Rev. 5:1989;81-92.
    • (1989) FEMS Microbiol. Rev. , vol.5 , pp. 81-92
    • Lengeler, J.W.1    Vogler, A.P.2
  • 13
    • 0028534956 scopus 로고
    • Enzymes II of the phospho-enolpyruvate-dependent phosphotransferase systems: Their structure and function in carbohydrate transport
    • Lengeler J. W., Jahreis K., Wehmeier U. F. Enzymes II of the phospho-enolpyruvate-dependent phosphotransferase systems: their structure and function in carbohydrate transport. Biochim. Biophys. Acta, 1188:1994;1-28.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 1-28
    • Lengeler, J.W.1    Jahreis, K.2    Wehmeier, U.F.3
  • 14
    • 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. Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2 Å resolution. Biochemistry. 30:1991;9583-9594.
    • (1991) Biochemistry , vol.30 , pp. 9583-9594
    • Liao, D.I.1    Kapadia, G.2    Reddy, P.3    Saier M.H., Jr.4    Reizer, J.5    Herzberg, O.6
  • 15
    • 0030586030 scopus 로고    scopus 로고
    • The first step in sugar transport: Crystal structure of the amino terminal domain of enzyme I 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. The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the Escherichia coli PEP: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr. Structure. 4:1996;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
  • 17
    • 0032516824 scopus 로고    scopus 로고
    • The thermal stability and domain interactions of the mannitol permease of Escherichia coli. A differential scanning calorimetry study
    • Meijberg W., Schuurman-Wolters G. K., Boer H., Scheek R. M., Robillard G. T. The thermal stability and domain interactions of the mannitol permease of Escherichia coli. A differential scanning calorimetry study. J. Biol. Chem. 273:1998;20785-20794.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20785-20794
    • Meijberg, W.1    Schuurman-Wolters, G.K.2    Boer, H.3    Scheek, R.M.4    Robillard, G.T.5
  • 18
    • 0019122765 scopus 로고
    • Solubilization and reconstitution of the lactose transport system from Escherichia coli
    • Newman M. J., Wilson T. H. Solubilization and reconstitution of the lactose transport system from Escherichia coli. J. Biol. Chem. 255:1980;10583-10586.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10583-10586
    • Newman, M.J.1    Wilson, T.H.2
  • 20
    • 0032127262 scopus 로고    scopus 로고
    • Automation of specimen selection and data acquisition for protein electron crystallography
    • Oostergetel G. T., Keegstra W., Brisson A. Automation of specimen selection and data acquisition for protein electron crystallography. Ultramicroscopy. 74:1998;47-32.
    • (1998) Ultramicroscopy , vol.74 , pp. 47-32
    • Oostergetel, G.T.1    Keegstra, W.2    Brisson, A.3
  • 21
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C. N., Vajdos F., Fee L., Grimsley G., Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4:1995;2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 22
    • 0023661104 scopus 로고
    • Bacterial phosphoenolpyruvate-dependent phosphotransferase system: Association state of membrane-bound mannitol-specific enzyme II demonstrated by inactivation
    • Pas H. H., Ellory J. C., Robillard G. T. Bacterial phosphoenolpyruvate-dependent phosphotransferase system: association state of membrane-bound mannitol-specific enzyme II demonstrated by inactivation. Biochemistry. 26:1987;6689-6696.
    • (1987) Biochemistry , vol.26 , pp. 6689-6696
    • Pas, H.H.1    Ellory, J.C.2    Robillard, G.T.3
  • 23
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate carbohydrate phosphotransferase systems of bacteria
    • Postma P. W., Lengeler J. W., Jacobson G. R. Phosphoenolpyruvate carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57:1993;543-594.
    • (1993) Microbiol. Rev. , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 24
    • 0025233875 scopus 로고
    • Signal transduction by the bacterial phosphotransferase system. Diauxie and the crr gene
    • Roseman S., Meadow N. D. Signal transduction by the bacterial phosphotransferase system. Diauxie and the crr gene. J. Biol. Chem. 265:1990;2993-2996.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2993-2996
    • Roseman, S.1    Meadow, N.D.2
  • 25
    • 0028104094 scopus 로고
    • The bacterial phosphotransferase system: New frontiers 30 years later
    • Saier M. H. Jr, Reizer J. The bacterial phosphotransferase system: new frontiers 30 years later. Mol. Microbiol. 13:1994;755-764.
    • (1994) Mol. Microbiol. , vol.13 , pp. 755-764
    • Saier M.H., Jr.1    Reizer, J.2
  • 27
    • 0030753823 scopus 로고    scopus 로고
    • Subunit and amino acid interactions in the Escherichia coli mannitol permease: A functional complementation study of coexpressed mutant permease proteins
    • Saraceni-Richards C. A., Jacobson G. R. Subunit and amino acid interactions in the Escherichia coli mannitol permease: a functional complementation study of coexpressed mutant permease proteins. J. Bacteriol. 179:1997;5171-5177.
    • (1997) J. Bacteriol. , vol.179 , pp. 5171-5177
    • Saraceni-Richards, C.A.1    Jacobson, G.R.2
  • 28
    • 0032570740 scopus 로고    scopus 로고
    • Crystal structure of the IIB subunit of a fructose permease (IIBLev) from Bacillus subtilis
    • Schauder S., Nunn R. S., Lanz R., Erni B., Schirmer T. Crystal structure of the IIB subunit of a fructose permease (IIBLev) from Bacillus subtilis. J. Mol. Biol. 276:1998;591-602.
    • (1998) J. Mol. Biol. , vol.276 , pp. 591-602
    • Schauder, S.1    Nunn, R.S.2    Lanz, R.3    Erni, B.4    Schirmer, T.5
  • 29
    • 0030199093 scopus 로고    scopus 로고
    • Analysis of carbon film planarity by reflection light microscopy
    • Schmutz M., Brisson A. Analysis of carbon film planarity by reflection light microscopy. Ultramicroscopy. 63:1996;263-272.
    • (1996) Ultramicroscopy , vol.63 , pp. 263-272
    • Schmutz, M.1    Brisson, A.2
  • 30
    • 0030612122 scopus 로고    scopus 로고
    • The structure of enzyme IIA lactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system
    • Sliz P., Engelmann R., Hengstenberg W., Pai E. F. The structure of enzyme IIA lactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system. Structure. 5:1997;775-788.
    • (1997) Structure , vol.5 , pp. 775-788
    • Sliz, P.1    Engelmann, R.2    Hengstenberg, W.3    Pai, E.F.4
  • 31
    • 0026052185 scopus 로고
    • Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions
    • Sugiyama J. E., Mahmoodian S., Jacobson G. R. Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions. Proc. Natl Acad. Sci. USA. 88:1991;9603-9607.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9603-9607
    • Sugiyama, J.E.1    Mahmoodian, S.2    Jacobson, G.R.3
  • 32
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin P. N. T., Henderson R. Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94:1975;425-440.
    • (1975) J. Mol. Biol. , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 33
  • 34
    • 0032521383 scopus 로고    scopus 로고
    • The structure of the Escherichia coli phosphotransferase IIA mannitol reveals a novel fold with two conformations of the active site
    • van Montfort R. L. M., Pijning T., Kalk K. H., Hangyi I., Kouwijzer M. L., Robillard G. T., Dijkstra B. W. The structure of the Escherichia coli phosphotransferase IIA mannitol reveals a novel fold with two conformations of the active site. Structure. 6:1998;377-388.
    • (1998) Structure , vol.6 , pp. 377-388
    • Van Montfort, R.L.M.1    Pijning, T.2    Kalk, K.H.3    Hangyi, I.4    Kouwijzer, M.L.5    Robillard, G.T.6    Dijkstra, B.W.7
  • 35
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:1992;487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1


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