메뉴 건너뛰기




Volumn 16, Issue 6, 2007, Pages 1032-1041

Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures

Author keywords

Atomic resolution; Chemotaxis; Exo anomeric effect; Hinge motion; Radiation damage

Indexed keywords

ALLOSE; CARBON DIOXIDE; GALAPTIN; GLUCOSE; HYDROGEN; LIGAND; RIBOSE;

EID: 34249781722     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062707807     Document Type: Article
Times cited : (94)

References (61)
  • 1
    • 0014409297 scopus 로고
    • Transport of sugars and amino acids in bacteria. I. Purification and specificity of the galactose- and leucine-binding proteins
    • Anraku, Y. 1968. Transport of sugars and amino acids in bacteria. I. Purification and specificity of the galactose- and leucine-binding proteins. J. Biol. Chem. 243: 3116-3122.
    • (1968) J. Biol. Chem , vol.243 , pp. 3116-3122
    • Anraku, Y.1
  • 2
    • 0033636314 scopus 로고    scopus 로고
    • Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core
    • Armstrong, N. and Gouaux, E. 2000. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core. Neuron 28: 165-181.
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 3
    • 16644367850 scopus 로고    scopus 로고
    • Structural effects of radiation damage and its potential for phasing
    • Banumathi, S., Zwart, P.H., Ramagopal, U.A., Dauter, M., and Dauter, Z. 2004. Structural effects of radiation damage and its potential for phasing. Acta Crystallogr. 60D: 1085-1093.
    • (2004) Acta Crystallogr , vol.60 D , pp. 1085-1093
    • Banumathi, S.1    Zwart, P.H.2    Ramagopal, U.A.3    Dauter, M.4    Dauter, Z.5
  • 5
    • 23744489602 scopus 로고    scopus 로고
    • On the generalized valence bond description of the anomeric and exo-anomeric effects: An ab initio conformational study of 2-methoxytetrahydropyran
    • Bitzer, R.S., Barbosa, A.G., da Silva, C.O., and Nascimento, M.A. 2005. On the generalized valence bond description of the anomeric and exo-anomeric effects: An ab initio conformational study of 2-methoxytetrahydropyran. Carbohydr. Res. 340: 2171-2184.
    • (2005) Carbohydr. Res , vol.340 , pp. 2171-2184
    • Bitzer, R.S.1    Barbosa, A.G.2    da Silva, C.O.3    Nascimento, M.A.4
  • 6
    • 0032511137 scopus 로고    scopus 로고
    • Multiple open forms of ribose-binding protein trace the path of its conformational change
    • Bjorkman, A.J. and Mowbray, S.L. 1998. Multiple open forms of ribose-binding protein trace the path of its conformational change. J. Mol. Biol. 279: 651-664.
    • (1998) J. Mol. Biol , vol.279 , pp. 651-664
    • Bjorkman, A.J.1    Mowbray, S.L.2
  • 7
    • 0026597444 scopus 로고
    • Free R-Value - A novel statistical quantity for assessing the accuracy of crystal-structures
    • Brunger, 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
    • Brunger, A.T.1
  • 8
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A., Adams, P., Clore, M., Gros, P., Nilges, M., and Read, R. 1998. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D54: 905-921.
    • (1998) Acta Crystallogr , vol.D54 , pp. 905-921
    • Brunger, A.1    Adams, P.2    Clore, M.3    Gros, P.4    Nilges, M.5    Read, R.6
  • 9
    • 0034055545 scopus 로고    scopus 로고
    • Structural changes in a cryo-cooled protein crystal owing to radiation damage
    • Burmeister, W.P. 2000. Structural changes in a cryo-cooled protein crystal owing to radiation damage. Acta Crystallogr. 56A: 328-341.
    • (2000) Acta Crystallogr , vol.56 A , pp. 328-341
    • Burmeister, W.P.1
  • 10
    • 0028929925 scopus 로고
    • Large-amplitude twisting motions of an interdomain hinge: A disulfide trapping study of the galactose-glucose binding protein
    • Careaga, C.L., Sutherland, J., Sabeti, J., and Falke, J.J. 1995. Large-amplitude twisting motions of an interdomain hinge: A disulfide trapping study of the galactose-glucose binding protein. Biochemistry 34: 3048-3055.
    • (1995) Biochemistry , vol.34 , pp. 3048-3055
    • Careaga, C.L.1    Sutherland, J.2    Sabeti, J.3    Falke, J.J.4
  • 11
    • 0033548701 scopus 로고    scopus 로고
    • Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8 Å resolution
    • Chaudhuri, B.N., Ko, J., Park, C., Jones, T.A., and Mowbray, S.L. 1999. Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8 Å resolution. J. Mol. Biol. 286: 1519-1531.
    • (1999) J. Mol. Biol , vol.286 , pp. 1519-1531
    • Chaudhuri, B.N.1    Ko, J.2    Park, C.3    Jones, T.A.4    Mowbray, S.L.5
  • 13
    • 21644436120 scopus 로고    scopus 로고
    • Pros and cons of cryocrystallography: Should we also collect a room-temperature data set?
    • Dunlop, K.V., Irvin, R.T., and Hazes, B. 2005. Pros and cons of cryocrystallography: Should we also collect a room-temperature data set? Acta Crystallogr. 61D: 80-87.
    • (2005) Acta Crystallogr , vol.61 D , pp. 80-87
    • Dunlop, K.V.1    Irvin, R.T.2    Hazes, B.3
  • 14
    • 33544461370 scopus 로고    scopus 로고
    • The Venus flytrap of periplasmic binding proteins: An ancient protein module present in multiple drug receptors
    • Felder, C.B., Graul, R.C., Lee, A.Y., Merkle, H.P., and Sadee, W. 1999. The Venus flytrap of periplasmic binding proteins: An ancient protein module present in multiple drug receptors. AAPS PharmSci 1: E2.
    • (1999) AAPS PharmSci , vol.1
    • Felder, C.B.1    Graul, R.C.2    Lee, A.Y.3    Merkle, H.P.4    Sadee, W.5
  • 15
    • 0028002085 scopus 로고
    • The 1.9 Ångstrom X-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium
    • Flocco, M.M. and Mowbray, S.L. 1994. The 1.9 Ångstrom X-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium. J. Biol. Chem. 269: 8931-8936.
    • (1994) J. Biol. Chem , vol.269 , pp. 8931-8936
    • Flocco, M.M.1    Mowbray, S.L.2
  • 16
    • 0028972304 scopus 로고
    • C α-based torsion angles: A simple tool to analyze protein conformational changes
    • Flocco, M.M. and Mowbray, S.L. 1995. C α-based torsion angles: A simple tool to analyze protein conformational changes. Protein Sci. 4: 2118-2122.
    • (1995) Protein Sci , vol.4 , pp. 2118-2122
    • Flocco, M.M.1    Mowbray, S.L.2
  • 17
    • 0033548125 scopus 로고    scopus 로고
    • Domain dislocation: A change of core structure in periplasmic binding proteins in their evolutionary history
    • Fukami-Kobayashi, K., Tateno, Y., and Nishikawa, K. 1999. Domain dislocation: A change of core structure in periplasmic binding proteins in their evolutionary history. J. Mol. Biol. 286: 279-290.
    • (1999) J. Mol. Biol , vol.286 , pp. 279-290
    • Fukami-Kobayashi, K.1    Tateno, Y.2    Nishikawa, K.3
  • 18
    • 0037011939 scopus 로고    scopus 로고
    • Inter-receptor communication through arrays of bacterial chemoreceptors
    • Gestwicki, J.E. and Kiessling, L.L. 2002. Inter-receptor communication through arrays of bacterial chemoreceptors. Nature (London) 415: 81-84.
    • (2002) Nature (London) , vol.415 , pp. 81-84
    • Gestwicki, J.E.1    Kiessling, L.L.2
  • 19
    • 0033827123 scopus 로고    scopus 로고
    • Tuning chemotactic responses with synthetic multivalent ligands
    • Gestwicki, J.E., Strong, L.E., and Kiessling, L.L. 2000. Tuning chemotactic responses with synthetic multivalent ligands. Chem. Biol. 7: 583-591.
    • (2000) Chem. Biol , vol.7 , pp. 583-591
    • Gestwicki, J.E.1    Strong, L.E.2    Kiessling, L.L.3
  • 21
    • 0036305965 scopus 로고    scopus 로고
    • Atomic (0.94 Ångstrom) resolution structure of an inverting glycosidase in complex with substrate
    • Guerin, D.M.A., Lascombe, M.B., Costabel, M., Souchon, H., Lamzin, V., Beguin, P., and Alzari, P.M. 2002. Atomic (0.94 Ångstrom) resolution structure of an inverting glycosidase in complex with substrate. J. Mol. Biol. 316: 1061-1069.
    • (2002) J. Mol. Biol , vol.316 , pp. 1061-1069
    • Guerin, D.M.A.1    Lascombe, M.B.2    Costabel, M.3    Souchon, H.4    Lamzin, V.5    Beguin, P.6    Alzari, P.M.7
  • 22
    • 0032769661 scopus 로고    scopus 로고
    • Structural principles governing domain motions in proteins
    • Hayward, S. 1999. Structural principles governing domain motions in proteins. Proteins 36: 425-435.
    • (1999) Proteins , vol.36 , pp. 425-435
    • Hayward, S.1
  • 23
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • Hayward, S. and Berendsen, H.J. 1998. Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme. Proteins 30: 144-154.
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 24
    • 0015238086 scopus 로고
    • Role of galactose-binding protein in chemotaxis of Escherichia coli toward galactose
    • Hazelbauer, G.L. and Adler, J. 1971. Role of galactose-binding protein in chemotaxis of Escherichia coli toward galactose. Nat. New Biol. 230: 101-104.
    • (1971) Nat. New Biol , vol.230 , pp. 101-104
    • Hazelbauer, G.L.1    Adler, J.2
  • 25
    • 0001490896 scopus 로고
    • The conformational properties of glycosidic linkages
    • Lemieux, R.U. and Koto, S. 1974. The conformational properties of glycosidic linkages. Tetrahedron 30: 1933-1944.
    • (1974) Tetrahedron , vol.30 , pp. 1933-1944
    • Lemieux, R.U.1    Koto, S.2
  • 26
    • 0001339474 scopus 로고
    • Solvation effects on conformational equilibrium studies related to methyl glycopyranosides
    • Lemieux, R.U., Pavia, A.A., Martin, J.C., and Watanabe, K.A. 1969. Solvation effects on conformational equilibrium studies related to methyl glycopyranosides. Can. J. Chem. 47: 4427-4439.
    • (1969) Can. J. Chem , vol.47 , pp. 4427-4439
    • Lemieux, R.U.1    Pavia, A.A.2    Martin, J.C.3    Watanabe, K.A.4
  • 27
    • 0038752617 scopus 로고    scopus 로고
    • Computational design of receptor and sensor proteins with novel functions
    • Looger, L.L., Dwyer, M.A., Smith, J.J., and Hellinga, H.W. 2003. Computational design of receptor and sensor proteins with novel functions. Nature 423: 185-190.
    • (2003) Nature , vol.423 , pp. 185-190
    • Looger, L.L.1    Dwyer, M.A.2    Smith, J.J.3    Hellinga, H.W.4
  • 28
    • 0034479757 scopus 로고    scopus 로고
    • TOP: A new method for protein structure comparisons and similarity searches
    • Lu, G. 2000. TOP: A new method for protein structure comparisons and similarity searches. J. Appl. Crystallogr. 33: 176-183.
    • (2000) J. Appl. Crystallogr , vol.33 , pp. 176-183
    • Lu, G.1
  • 29
    • 0025922013 scopus 로고
    • 19F NMR studies of the D-galactose chemosensory receptor. 1. Sugar binding yields a global structural change
    • Luck, L.A. and Falke, J.J. 1991a. 19F NMR studies of the D-galactose chemosensory receptor. 1. Sugar binding yields a global structural change. Biochemistry 30: 4248-4256.
    • (1991) Biochemistry , vol.30 , pp. 4248-4256
    • Luck, L.A.1    Falke, J.J.2
  • 30
    • 0025821340 scopus 로고
    • Open conformation of a substrate-binding cleft: 19F NMR studies of cleft angle in the D-galactose chemosensory receptor
    • Luck, L.A. and Falke, J.J. 1991b. Open conformation of a substrate-binding cleft: 19F NMR studies of cleft angle in the D-galactose chemosensory receptor. Biochemistry 30: 6484-6490.
    • (1991) Biochemistry , vol.30 , pp. 6484-6490
    • Luck, L.A.1    Falke, J.J.2
  • 31
    • 0037134514 scopus 로고    scopus 로고
    • Hinge-bending motion of D-allose-binding protein from Escherichia coli: Three open conformations
    • Magnusson, U., Chaudhuri, B.N., Ko, J., Park, C., Jones, T.A., and Mowbray, S.L. 2002. Hinge-bending motion of D-allose-binding protein from Escherichia coli: Three open conformations. J. Biol. Chem. 277: 14077-14084.
    • (2002) J. Biol. Chem , vol.277 , pp. 14077-14084
    • Magnusson, U.1    Chaudhuri, B.N.2    Ko, J.3    Park, C.4    Jones, T.A.5    Mowbray, S.L.6
  • 32
    • 1542365360 scopus 로고    scopus 로고
    • X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity
    • Magnusson, U., Salopek-Sondi, B., Luck, L.A., and Mowbray, S.L. 2004. X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity. J. Biol. Chem. 279: 8747-8752.
    • (2004) J. Biol. Chem , vol.279 , pp. 8747-8752
    • Magnusson, U.1    Salopek-Sondi, B.2    Luck, L.A.3    Mowbray, S.L.4
  • 33
    • 0036452022 scopus 로고    scopus 로고
    • Specific damage induced by X-ray radiation and structural changes in the primary photoreaction of bacteriorhodopsin
    • Matsui, Y., Sakai, K., Murakami, M., Shiro, Y., Adachi, S., Okumura, H., and Kouyama, T. 2002. Specific damage induced by X-ray radiation and structural changes in the primary photoreaction of bacteriorhodopsin. J. Mol. Biol. 324: 469-481.
    • (2002) J. Mol. Biol , vol.324 , pp. 469-481
    • Matsui, Y.1    Sakai, K.2    Murakami, M.3    Shiro, Y.4    Adachi, S.5    Okumura, H.6    Kouyama, T.7
  • 36
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee, D.E. 1999. XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125: 156-165.
    • (1999) J. Struct. Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 37
    • 0018948077 scopus 로고
    • The mechanism of sugar binding to the periplasmic receptor for galactose chemotaxis and transport in Escherichia coli
    • Miller, D.M., Olson, J.S., and Quiocho, F.A. 1980. The mechanism of sugar binding to the periplasmic receptor for galactose chemotaxis and transport in Escherichia coli. J. Biol. Chem. 255: 2465-2471.
    • (1980) J. Biol. Chem , vol.255 , pp. 2465-2471
    • Miller, D.M.1    Olson, J.S.2    Quiocho, F.A.3
  • 38
    • 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., and Quiocho, F.A. 1983. Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis. J. Biol. Chem. 258: 3665-3672.
    • (1983) J. Biol. Chem , vol.258 , pp. 3665-3672
    • Miller, D.M.1    Olson, J.S.2    Pflugrath, J.W.3    Quiocho, F.A.4
  • 39
    • 0027112289 scopus 로고
    • 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli
    • Mowbray, S.L. and 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
  • 40
    • 0025574192 scopus 로고
    • Structure of the periplasmic glucose/galactose receptor of Salmonella typhimurium
    • Mowbray, S.L., Smith, R.D., and Cole, L.B. 1990. Structure of the periplasmic glucose/galactose receptor of Salmonella typhimurium. Receptor 1: 41-53.
    • (1990) Receptor , vol.1 , pp. 41-53
    • Mowbray, S.L.1    Smith, R.D.2    Cole, L.B.3
  • 41
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr. 50A: 157-163.
    • (1994) Acta Crystallogr , vol.50 A , pp. 157-163
    • Navaza, J.1
  • 42
    • 19444366428 scopus 로고    scopus 로고
    • Regulation of LuxPQ receptor activity by the quorum-sensing signal autoinducer-2
    • Neiditch, M.B., Federle, M.J., Miller, S.T., Bassler, B.L., and Hughson, F.M. 2005. Regulation of LuxPQ receptor activity by the quorum-sensing signal autoinducer-2. Mol. Cell 18: 507-518.
    • (2005) Mol. Cell , vol.18 , pp. 507-518
    • Neiditch, M.B.1    Federle, M.J.2    Miller, S.T.3    Bassler, B.L.4    Hughson, F.M.5
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • eds. C.W. Carter Jr. and R.M. Sweet, pp, Academic Press, San Diego, CA
    • Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. In Macromolecular Crystallography, Pt A (eds. C.W. Carter Jr. and R.M. Sweet), pp. 307-326. Academic Press, San Diego, CA.
    • (1997) Macromolecular Crystallography, Pt A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 0346732297 scopus 로고    scopus 로고
    • Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-Å resolution
    • Parthasarathy, S., Eaazhisai, K., Balaram, H., Balaram, P., and Murthy, M.R. 2003. Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-Å resolution. J. Biol. Chem. 278: 52461-52470.
    • (2003) J. Biol. Chem , vol.278 , pp. 52461-52470
    • Parthasarathy, S.1    Eaazhisai, K.2    Balaram, H.3    Balaram, P.4    Murthy, M.R.5
  • 45
  • 46
    • 0024511371 scopus 로고
    • Structure of the 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., and Quiocho, F.A. 1989. Structure of the 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
  • 47
    • 0035399396 scopus 로고    scopus 로고
    • A novel reagentless sensing system for measuring glucose based on the galactose/glucose-binding protein
    • Salins, L.L.E., Ware, R.A., Ensor, C.M., and Daunert, S. 2001. A novel reagentless sensing system for measuring glucose based on the galactose/glucose-binding protein. Anal. Biochem. 294: 19-26.
    • (2001) Anal. Biochem , vol.294 , pp. 19-26
    • Salins, L.L.E.1    Ware, R.A.2    Ensor, C.M.3    Daunert, S.4
  • 49
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • Sheldrick, G.M. and Schneider, T.R. 1997. SHELXL: High-resolution refinement. Methods Enzymol. 277: 319-343.
    • (1997) Methods Enzymol , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 50
    • 0030606240 scopus 로고    scopus 로고
    • Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: The maltose-, glucose/galactose- and ribose-binding proteins
    • Shilton, B.H., Flocco, M.M., Nilsson, M., and Mowbray, S.L. 1996. Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: The maltose-, glucose/galactose- and ribose-binding proteins. J. Mol. Biol. 264: 350-363.
    • (1996) J. Mol. Biol , vol.264 , pp. 350-363
    • Shilton, B.H.1    Flocco, M.M.2    Nilsson, M.3    Mowbray, S.L.4
  • 51
    • 3042613550 scopus 로고    scopus 로고
    • Likelihood-enhanced fast rotation functions
    • Storoni, L.C., McCoy, A.J., and Read, R.J. 2004. Likelihood-enhanced fast rotation functions. Acta Crystallogr. 60D: 432-438.
    • (2004) Acta Crystallogr , vol.60 D , pp. 432-438
    • Storoni, L.C.1    McCoy, A.J.2    Read, R.J.3
  • 52
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R. and Saier, M.H. 1993. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57: 320-346.
    • (1993) Microbiol. Rev , vol.57 , pp. 320-346
    • Tam, R.1    Saier, M.H.2
  • 53
    • 0141446029 scopus 로고    scopus 로고
    • Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants
    • Telmer, P.G. and Shilton, B.H. 2003. Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants. J. Biol. Chem. 278: 34555-34567.
    • (2003) J. Biol. Chem , vol.278 , pp. 34555-34567
    • Telmer, P.G.1    Shilton, B.H.2
  • 54
    • 17844398488 scopus 로고    scopus 로고
    • Ligand-free and -bound structures of the binding protein (LivJ) of the Escherichia coli ABC leucine/isoleucine/valine transport system: Trajectory and dynamics of the interdomain rotation and ligand specificity
    • Trakhanov, S., Vyas, N.K., Luecke, H., Kristensen, D.M., Ma, J., and Quiocho, F.A. 2005. Ligand-free and -bound structures of the binding protein (LivJ) of the Escherichia coli ABC leucine/isoleucine/valine transport system: Trajectory and dynamics of the interdomain rotation and ligand specificity. Biochemistry 44: 6597-6608.
    • (2005) Biochemistry , vol.44 , pp. 6597-6608
    • Trakhanov, S.1    Vyas, N.K.2    Luecke, H.3    Kristensen, D.M.4    Ma, J.5    Quiocho, F.A.6
  • 55
    • 0020742669 scopus 로고
    • The 3 Ångstrom resolution structure of a D-galactose-binding protein for transport and chemotaxis in Escherichia coli
    • Vyas, N.K., Vyas, M.N., and Quiocho, F.A. 1983. The 3 Ångstrom resolution structure of a D-galactose-binding protein for transport and chemotaxis in Escherichia coli. Biochemistry 80: 1792-1796.
    • (1983) Biochemistry , vol.80 , pp. 1792-1796
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 56
    • 0023256886 scopus 로고
    • A novel calcium-binding site in the galactose-binding protein of bacterial transport and chemotaxis
    • Vyas, N.K., Vyas, M.N., and Quiocho, F.A. 1987. A novel calcium-binding site in the galactose-binding protein of bacterial transport and chemotaxis. Nature 327: 635-638.
    • (1987) Nature , vol.327 , pp. 635-638
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 57
    • 0024237631 scopus 로고
    • Sugar and signal-transducer binding-sites of the Escherichia coli galactose chemoreceptor protein
    • Vyas, N.K., Vyas, M.N., and 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
  • 58
    • 0028244277 scopus 로고
    • Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose
    • Vyas, N.K., Vyas, M.N., and Quiocho, F.A. 1994. Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose. Biochemistry 33: 4762-4768.
    • (1994) Biochemistry , vol.33 , pp. 4762-4768
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 59
    • 0031179495 scopus 로고    scopus 로고
    • A low energy short hydrogen bond in very high resolution structures of protein receptor-phosphate complexes
    • Wang, Z., Luecke, H., Yao, N., and Quiocho, F.A. 1997. A low energy short hydrogen bond in very high resolution structures of protein receptor-phosphate complexes. Nat. Struct. Biol. 4: 519-522.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 519-522
    • Wang, Z.1    Luecke, H.2    Yao, N.3    Quiocho, F.A.4
  • 60
    • 0036591656 scopus 로고    scopus 로고
    • Cation-π interactions in ligand recognition and catalysis
    • Zacharias, N. and Dougherty, D.A. 2002. Cation-π interactions in ligand recognition and catalysis. Trends Pharmacol. Sci. 23: 281-287.
    • (2002) Trends Pharmacol. Sci , vol.23 , pp. 281-287
    • Zacharias, N.1    Dougherty, D.A.2
  • 61
    • 0027340581 scopus 로고
    • The 1.7 Ångstrom refined X-ray structure of the periplasmic glucose galactose receptor from Salmonella typhimurium
    • Zou, J.Y., Flocco, M.M., and Mowbray, S.L. 1993. The 1.7 Ångstrom refined X-ray structure of the periplasmic glucose galactose receptor from Salmonella typhimurium. J. Mol. Biol. 233: 739-752.
    • (1993) J. Mol. Biol , vol.233 , pp. 739-752
    • Zou, J.Y.1    Flocco, M.M.2    Mowbray, S.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.