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Volumn 262, Issue 2, 1996, Pages 225-242

The crystal structure of glutamine-binding protein from Escherichia coli

Author keywords

Crystal structure; Glutamine binding protein; Ligand binding; Periplasmic binding proteins; X ray crystallography

Indexed keywords

BINDING PROTEIN; GLUTAMINE;

EID: 0030595368     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0509     Document Type: Article
Times cited : (152)

References (49)
  • 1
    • 0022555851 scopus 로고
    • Bacterial periplasmic transport systems: Structure, mechanism, and evolution
    • Ames, G. F.-L. (1986). Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu. Rev. Biochem. 55, 397-425.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 397-425
    • Ames, G.F.-L.1
  • 3
    • 85027779617 scopus 로고
    • A system for collection and on-line integration of X-ray diffraction data from a multiwire area detector
    • Blum, M., Metcalf, P., Harrison, S. C. & Wiley, D. C. (1987). A system for collection and on-line integration of X-ray diffraction data from a multiwire area detector. J. Appl. Crystallog. 20, 235-242.
    • (1987) J. Appl. Crystallog. , vol.20 , pp. 235-242
    • Blum, M.1    Metcalf, P.2    Harrison, S.C.3    Wiley, D.C.4
  • 4
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 5
    • 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
  • 7
    • 0025805918 scopus 로고
    • Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 Å determined from the use of the single-wavelength anomalous scattering signal of an incorporated iodine atom
    • Chen, L., Rose, J. P., Breslow, E., Yang, D., Chang, W. R., Yoo, C. S., Furey, W. F. Jr, Sax, M. & Wang, B. C. (1991). Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 Å determined from the use of the single-wavelength anomalous scattering signal of an incorporated iodine atom. Proc. Natl Acad. Sci. USA, 88, 4240-4244.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 4240-4244
    • Chen, L.1    Rose, J.P.2    Breslow, E.3    Yang, D.4    Chang, W.R.5    Yoo, C.S.6    Furey W.F., Jr.7    Sax, M.8    Wang, B.C.9
  • 8
    • 0023084055 scopus 로고
    • Progressive sequence alignment as a prerequisite to correct phylogenetic trees
    • Feng, D. F. & Doolittle, R. F. (1987). Progressive sequence alignment as a prerequisite to correct phylogenetic trees. J. Mol. Evol. 25, 351-360.
    • (1987) J. Mol. Evol. , vol.25 , pp. 351-360
    • Feng, D.F.1    Doolittle, R.F.2
  • 9
    • 0001652118 scopus 로고
    • Crystallographic computing on an array processor
    • Furey, W. F., Wang, B. C. & Sax, M. (1982). Crystallographic computing on an array processor. J. Appl. Crystallog. 21, 160-166.
    • (1982) J. Appl. Crystallog. , vol.21 , pp. 160-166
    • Furey, W.F.1    Wang, B.C.2    Sax, M.3
  • 10
    • 0019178121 scopus 로고
    • Thermodynamic studies of binding proteins: Effect of temperature variations on substrate binding and conformation of the leucine-isoleucine-valine binding protein of Escherichia coli
    • Gaudin, C., Marty, B., Ragot, M., Sari, J. C. & Belaich, J. P. (1980). Thermodynamic studies of binding proteins: effect of temperature variations on substrate binding and conformation of the leucine-isoleucine-valine binding protein of Escherichia coli. Biochimie, 62, 741-746.
    • (1980) Biochimie , vol.62 , pp. 741-746
    • Gaudin, C.1    Marty, B.2    Ragot, M.3    Sari, J.C.4    Belaich, J.P.5
  • 11
    • 0019486502 scopus 로고
    • Structure of the L-arabinose-binding protein from Escherichia coli at 2.4 Å resolution
    • Gilliland, G. L. & Quiocho, F. A. (1981). Structure of the L-arabinose-binding protein from Escherichia coli at 2.4 Å resolution. J. Mol. Biol. 146, 341-362.
    • (1981) J. Mol. Biol. , vol.146 , pp. 341-362
    • Gilliland, G.L.1    Quiocho, F.A.2
  • 12
    • 0022293584 scopus 로고
    • Multiwire area X-ray diffractometers
    • Hamlin, R. (1985). Multiwire area X-ray diffractometers. Methods Enzymol. 114, 416-452.
    • (1985) Methods Enzymol. , vol.114 , pp. 416-452
    • Hamlin, R.1
  • 13
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macro-molecular structures
    • Hendrickson, W. A. (1985). Stereochemically restrained refinement of macro-molecular structures. Methods Enzymol. 115, 252-270.
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 14
    • 0027993652 scopus 로고
    • An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR
    • Hing, A. W., Tjandra, N., Cottam, P. F., Schaefer, J. & Ho, C. (1994). An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR. Biochemistry, 33, 8651-8661.
    • (1994) Biochemistry , vol.33 , pp. 8651-8661
    • Hing, A.W.1    Tjandra, N.2    Cottam, P.F.3    Schaefer, J.4    Ho, C.5
  • 15
    • 0022326269 scopus 로고
    • Software for a diffractometer with multiwire area detector
    • Howard, A. J., Nielsen, C. & Xuong, N. H. (1985). Software for a diffractometer with multiwire area detector. Methods Enzymol. 114, 452-472.
    • (1985) Methods Enzymol. , vol.114 , pp. 452-472
    • Howard, A.J.1    Nielsen, C.2    Xuong, N.H.3
  • 17
    • 0027956535 scopus 로고
    • Crystals of glutamine-binding protein in various conformational states
    • Hsiao, C. D., Sun, Y. J., Rose, J., Cottam, P. F., Ho, C. & Wang, B.-C. (1994). Crystals of glutamine-binding protein in various conformational states. J. Mol. Biol. 240, 87-91.
    • (1994) J. Mol. Biol. , vol.240 , pp. 87-91
    • Hsiao, C.D.1    Sun, Y.J.2    Rose, J.3    Cottam, P.F.4    Ho, C.5    Wang, B.-C.6
  • 18
    • 0019877776 scopus 로고
    • The reconstitution of binding protein-dependent active transport of glutamine in isolated membrane vesicles from Escherichia coli
    • Hunt, A. G. & Hong, J.-S. (1981). The reconstitution of binding protein-dependent active transport of glutamine in isolated membrane vesicles from Escherichia coli. J. Biol. Chem. 256, 11988-11991.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11988-11991
    • Hunt, A.G.1    Hong, J.-S.2
  • 19
    • 0020639046 scopus 로고
    • Involvement of histidine and tryptophan residues of glutamine binding protein in the interaction with membrane-bound components of the glutamine transport system of Escherichia coli
    • Hunt, A. G. & Hong, J.-S. (1983). Involvement of histidine and tryptophan residues of glutamine binding protein in the interaction with membrane-bound components of the glutamine transport system of Escherichia coli. Biochemistry, 22, 851-854.
    • (1983) Biochemistry , vol.22 , pp. 851-854
    • Hunt, A.G.1    Hong, J.-S.2
  • 20
    • 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. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3
  • 21
    • 0026321096 scopus 로고
    • Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7 Å resolution
    • Kang, C.-F., Shin, W.-C., Yamagata, Y., Gokcen, S., Ames, F.-L. & Kim, S.-H. (1991). Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7 Å resolution. J. Biol. Chem. 266, 23893-23899.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23893-23899
    • Kang, C.-F.1    Shin, W.-C.2    Yamagata, Y.3    Gokcen, S.4    Ames, F.-L.5    Kim, S.-H.6
  • 22
    • 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. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 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 Crystallog. 26, 283-291.
    • (1993) J. Appl Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 24
    • 0001099937 scopus 로고
    • Traitements statistique des erreurs dans la determination des structures cristallines
    • Luzzati, P. V. (1952). Traitements statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5, 802-810.
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, P.V.1
  • 25
    • 0021062151 scopus 로고
    • Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis
    • Miller, D. M., Olson, J. S., Pflugrath, J. W. & Quiocho, F. A. (1983). Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis. J. Biol. Chem. 258, 13665-13672.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13665-13672
    • Miller, D.M.1    Olson, J.S.2    Pflugrath, J.W.3    Quiocho, F.A.4
  • 26
    • 0027112289 scopus 로고
    • 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli
    • Mowbray, S. L. & Cole, L. B. (1992). 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli. J. Mol. Biol. 225, 155-175.
    • (1992) J. Mol. Biol. , vol.225 , pp. 155-175
    • Mowbray, S.L.1    Cole, L.B.2
  • 27
    • 0029200246 scopus 로고
    • 2 Å Resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
    • Nickitenko, A. V., Trakhanov, S. & Quiocho, F. A. (1994). 2 Å Resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor. Biochemistry, 34, 16585-16594.
    • (1994) Biochemistry , vol.34 , pp. 16585-16594
    • Nickitenko, A.V.1    Trakhanov, S.2    Quiocho, F.A.3
  • 28
    • 0027235488 scopus 로고
    • Three-dimensional structure of the periplasmic lysine/arginine/ ornithine-binding protein with and without a ligand
    • Oh, B.-H., Pandit, J., Kang, C.-H., Nikaido, K., Gokcen, S., Ames, G. F.-L. & Kim, S.-H. (1993). Three-dimensional structure of the periplasmic lysine/arginine/ ornithine-binding protein with and without a ligand. J. Biol. Chem. 268, 11348-11355.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11348-11355
    • Oh, B.-H.1    Pandit, J.2    Kang, C.-H.3    Nikaido, K.4    Gokcen, S.5    Ames, G.F.-L.6    Kim, S.-H.7
  • 29
    • 0028067178 scopus 로고
    • The bacterial periplasmic histidine-binding protein structure/ function analysis of the ligand-binding site and comparison with related proteins
    • Oh, B.-H., Kang, C.-H., Bondt, H. D., Kim, S.-H. Nikaido, K., Joshi, A. K. & Ames, G. F.-L. (1994). The bacterial periplasmic histidine-binding protein structure/ function analysis of the ligand-binding site and comparison with related proteins. J. Biol. Chem. 269, 4135-4143.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4135-4143
    • Oh, B.-H.1    Kang, C.-H.2    Bondt, H.D.3    Kim, S.-H.4    Nikaido, K.5    Joshi, A.K.6    Ames, G.F.-L.7
  • 30
    • 0014961699 scopus 로고
    • Reversible conformational change in a leucine-binding protein from Escherichia coli
    • Penrose, W. R., Zand, R. & Oxender, D. L. (1970). Reversible conformational change in a leucine-binding protein from Escherichia coli. J. Biol. Chem. 245, 1432-1437.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1432-1437
    • Penrose, W.R.1    Zand, R.2    Oxender, D.L.3
  • 31
    • 0024278240 scopus 로고
    • The 2 Å resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium
    • Pflugrath, J. W. & Quiocho, F. A. (1988). The 2 Å resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium. J. Mol. Biol. 200, 163-180.
    • (1988) J. Mol. Biol. , vol.200 , pp. 163-180
    • Pflugrath, J.W.1    Quiocho, F.A.2
  • 32
    • 0025716317 scopus 로고
    • Atomic structure of periplasmic binding proteins and the high-affinity active transport systems in bacteria
    • Quiocho, F. A. (1990). Atomic structure of periplasmic binding proteins and the high-affinity active transport systems in bacteria. Phil. Trans. Roy. Soc. London, ser. B, 326, 341-351.
    • (1990) Phil. Trans. Roy. Soc. London, Ser. B , vol.326 , pp. 341-351
    • Quiocho, F.A.1
  • 33
    • 0015395720 scopus 로고
    • Antibody-mediated modification of the binding properties of a protein related to galactose transport
    • Rotman, B. & Ellis, J. H. (1972). Antibody-mediated modification of the binding properties of a protein related to galactose transport. J. Bacteriol. 111, 791-796.
    • (1972) J. Bacteriol. , vol.111 , pp. 791-796
    • Rotman, B.1    Ellis, J.H.2
  • 34
    • 0024563996 scopus 로고
    • Periplasmic binding protein structure and function: Refined X-ray structure of the leucine/isoleucine/valine-binding protein and its complex with leucine
    • Sack, J. S., Saper, M. A. & Quiocho, F. A. (1989a). Periplasmic binding protein structure and function: refined X-ray structure of the leucine/isoleucine/valine-binding protein and its complex with leucine. J. Mol. Biol. 206, 171-191.
    • (1989) J. Mol. Biol. , vol.206 , pp. 171-191
    • Sack, J.S.1    Saper, M.A.2    Quiocho, F.A.3
  • 35
    • 0024511371 scopus 로고
    • Structure of L-leucine-binding protein refined at 2.4 Å resolution and comparison with the Leu/Ile/Val-binding protein structure
    • Sack, J. S., Trakhanov, S. D., Tsigannik, I. H. & Quiocho, F. A. (1989b). Structure of L-leucine-binding protein refined at 2.4 Å resolution and comparison with the Leu/Ile/Val-binding protein structure. J. Mol. Biol. 206, 193-207.
    • (1989) J. Mol. Biol. , vol.206 , pp. 193-207
    • Sack, J.S.1    Trakhanov, S.D.2    Tsigannik, I.H.3    Quiocho, F.A.4
  • 36
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
    • Sharff, A. J., Rodseth, L. E., Spurlino, J. C. & Quiocho, F. A. (1992). Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry, 31, 10657-10663.
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 38
    • 0024816523 scopus 로고
    • Proton nuclear magnetic resonance studies on glutamine-binding protein from Escherichia coli: Formation of intermolecular and intramolecular hydrogen bonds upon ligand binding
    • Shen, Q., Simplaceanu, V., Cottam, P. F. & Ho, C. (1989a). Proton nuclear magnetic resonance studies on glutamine-binding protein from Escherichia coli: formation of intermolecular and intramolecular hydrogen bonds upon ligand binding. J. Mol. Biol. 210, 849-857.
    • (1989) J. Mol. Biol. , vol.210 , pp. 849-857
    • Shen, Q.1    Simplaceanu, V.2    Cottam, P.F.3    Ho, C.4
  • 39
    • 0024804621 scopus 로고
    • Molecular genetic, biochemical and nuclear magnetic resonance studies on the role of the tryptophan residues of glutamine-binding protein from Escherichia coli
    • Shen, Q., Simplaceanu, V., Cottam, P. F., Wu, J.-L., Hong, J.-S. & Ho, C. (1989b). Molecular genetic, biochemical and nuclear magnetic resonance studies on the role of the tryptophan residues of glutamine-binding protein from Escherichia coli. J. Mol. Biol. 210, 859-867.
    • (1989) J. Mol. Biol. , vol.210 , pp. 859-867
    • Shen, Q.1    Simplaceanu, V.2    Cottam, P.F.3    Wu, J.-L.4    Hong, J.-S.5    Ho, C.6
  • 40
    • 0025754301 scopus 로고
    • The 2.3 Å resolution structure of the maltose- or maltodextrin-binding protein, a primary acceptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., Lu, G.-Y. & Quiocho, F. A. (1991). The 2.3 Å resolution structure of the maltose- or maltodextrin-binding protein, a primary acceptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266, 5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.-Y.2    Quiocho, F.A.3
  • 41
    • 0022298619 scopus 로고
    • Constrained-restrained least-square (CORELS) refinement of proteins and nucleic acids
    • Sussman, J. L. (1985). Constrained-restrained least-square (CORELS) refinement of proteins and nucleic acids. Methods Enzymol. 115, 271-303.
    • (1985) Methods Enzymol. , vol.115 , pp. 271-303
    • Sussman, J.L.1
  • 44
    • 0024237631 scopus 로고
    • Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein
    • Vyas, N. K., Vyas, M. N. & Quiocho, F. A. (1988). Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein. Science, 242, 1290-1295.
    • (1988) Science , vol.242 , pp. 1290-1295
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 45
    • 0022325950 scopus 로고
    • Resolution of phase ambiguity in macromolecular crystallography
    • Wang, B.-C. (1985). Resolution of phase ambiguity in macromolecular crystallography. Methods Enzymol. 115, 90-112.
    • (1985) Methods Enzymol. , vol.115 , pp. 90-112
    • Wang, B.-C.1
  • 46
    • 0001694424 scopus 로고
    • A binding protein for glutamine and its relation to active transport in Escherichia coli
    • Weiner, J. H. & Heppel, L. A. (1971). A binding protein for glutamine and its relation to active transport in Escherichia coli. J. Biol. Chem. 246, 6933-6941.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6933-6941
    • Weiner, J.H.1    Heppel, L.A.2
  • 47
    • 0015011140 scopus 로고
    • A binding protein for L glutamine and its relation to active transport in E. coli
    • Weiner, J. H., Furlong, C. E. & Heppel, L. A. (1971). A binding protein for L glutamine and its relation to active transport in E. coli. Arch. Biochem. Biophys. 142, 715-717.
    • (1971) Arch. Biochem. Biophys. , vol.142 , pp. 715-717
    • Weiner, J.H.1    Furlong, C.E.2    Heppel, L.A.3
  • 48
    • 0001210234 scopus 로고
    • The probability distribution of X-ray intensities
    • Wilson, A. J. C. (1949). The probability distribution of X-ray intensities. Acta Crystallog. 2, 318-321.
    • (1949) Acta Crystallog. , vol.2 , pp. 318-321
    • Wilson, A.J.C.1
  • 49
    • 0028174670 scopus 로고
    • Refined 1.89 Å structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins
    • Yao, N., Trakhanov, S. & Quiocho, F. A. (1994). Refined 1.89 Å structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins. Biochemistry, 33, 4769-4779.
    • (1994) Biochemistry , vol.33 , pp. 4769-4779
    • Yao, N.1    Trakhanov, S.2    Quiocho, F.A.3


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