메뉴 건너뛰기




Volumn 44, Issue 17, 2005, Pages 6597-6608

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

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CRYSTAL STRUCTURE; ESCHERICHIA COLI; HYDROPHOBICITY; MOLECULAR DYNAMICS; PROTEINS;

EID: 17844398488     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047302o     Document Type: Article
Times cited : (85)

References (59)
  • 2
    • 0343603660 scopus 로고    scopus 로고
    • A functional-phylogenetic classification system for transmembrane solute transporters
    • Saier, M. H., Jr. (2000) A functional-phylogenetic classification system for transmembrane solute transporters, Microbiol. Mol. Biol. Rev. 64, 354-411.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 354-411
    • Saier Jr., M.H.1
  • 3
    • 0028337332 scopus 로고
    • Maltose transport system of Escherichia coli: An ABC-type transporter
    • Nikaido, H. (1994) Maltose transport system of Escherichia coli: an ABC-type transporter, FEBS Lett. 246, 55-58.
    • (1994) FEBS Lett. , vol.246 , pp. 55-58
    • Nikaido, H.1
  • 4
    • 0028294944 scopus 로고
    • Peptide transport by microorganisms
    • Payne, J. W., and Smith, M. W. (1994) Peptide transport by microorganisms, Adv. Microb. Physiol. 36, 1-80.
    • (1994) Adv. Microb. Physiol. , vol.36 , pp. 1-80
    • Payne, J.W.1    Smith, M.W.2
  • 5
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho, F. A., and Ledvina, P. S. (1996) Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes, Mol. Microbiol. 20, 17-25.
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 6
    • 0025353846 scopus 로고
    • Nucleotide sequence and genetic characterization reveal six essential genes for the LIV-I and LS transport systems of Escherichia coli
    • Adams, M. D., Wagner, L. M., Graddis, T. J., Landick, R., Antonucci, T. K., Gibson, A. L., and Oxender, D. L. (1990) Nucleotide sequence and genetic characterization reveal six essential genes for the LIV-I and LS transport systems of Escherichia coli, J. Biol. Chem. 265, 11436-11443.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11436-11443
    • Adams, M.D.1    Wagner, L.M.2    Graddis, T.J.3    Landick, R.4    Antonucci, T.K.5    Gibson, A.L.6    Oxender, D.L.7
  • 7
    • 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
  • 8
    • 0024563996 scopus 로고
    • Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine
    • Sack, J. S., Saper, M. A., and Quiocho, F. A. (1989) Periplasmic binding protein structure and function. Refined X-ray structures 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
  • 9
    • 0019486502 scopus 로고
    • Structure of the L-arabinose-binding protein from Escherichia coli at 2.4 Å resolution
    • Gilliland, G. L., and 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
  • 10
    • 0021205810 scopus 로고
    • Novel stereospecificity of the L-arabinose-binding protein
    • Quiocho, F. A., and Vyas, N. K. (1984) Novel stereospecificity of the L-arabinose-binding protein, Nature 310, 381-386.
    • (1984) Nature , vol.310 , pp. 381-386
    • Quiocho, F.A.1    Vyas, N.K.2
  • 11
    • 0020742669 scopus 로고
    • The 3 Å 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 Å resolution structure of a D-galactose-binding protein for transport and chemotaxis in Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 80, 1792-1796.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 1792-1796
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 12
    • 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
  • 13
    • 0020478556 scopus 로고
    • Hinge-bending in L-arabinose-binding protein: The "Venus's- flytrap" model
    • Mao, B., Pear, M. R., McCammon, J. A., and Quiocho, F. A. (1982) Hinge-bending in L-arabinose-binding protein: The "Venus's-flytrap" model, J. Biol. Chem. 257, 1131-1133.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1131-1133
    • Mao, B.1    Pear, M.R.2    McCammon, J.A.3    Quiocho, F.A.4
  • 14
    • 0029116404 scopus 로고
    • Influence of divalent cations in protein crystallization
    • Trakhanov, S., and Quiocho, F. A. (1995) Influence of divalent cations in protein crystallization, Protein Sci. 4, 1914-1919.
    • (1995) Protein Sci. , vol.4 , pp. 1914-1919
    • Trakhanov, S.1    Quiocho, F.A.2
  • 15
    • 0345189097 scopus 로고
    • Spectral properties of the leucine-isoleucine-valine binding protein and its complexes with substrates
    • Vorotyntseva, T. I., Surin, A. M., Trakhanov, S. D., Nabiev, I. R., and Antonov, V. K. (1981) Spectral properties of the leucine-isoleucine-valine binding protein and its complexes with substrates, Bioorg. Khim. 7, 45-57.
    • (1981) Bioorg. Khim. , vol.7 , pp. 45-57
    • Vorotyntseva, T.I.1    Surin, A.M.2    Trakhanov, S.D.3    Nabiev, I.R.4    Antonov, V.K.5
  • 16
    • 17844401027 scopus 로고
    • Merck Sharp & Dhome Laboratories, Rahway, NJ
    • Fitzgerald, P. M. D. (1988) MERLOT Manual, Merck Sharp & Dhome Laboratories, Rahway, NJ.
    • (1988) MERLOT Manual
    • Fitzgerald, P.M.D.1
  • 19
    • 0030818592 scopus 로고    scopus 로고
    • CHAIN - A crystallographic modeling program
    • Sack, J. S., and Quiocho, F. A. (1997) CHAIN - A crystallographic modeling program, Methods Enzymol. 277, 158-173.
    • (1997) Methods Enzymol. , vol.277 , pp. 158-173
    • Sack, J.S.1    Quiocho, F.A.2
  • 20
    • 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., and 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
  • 21
    • 0030852350 scopus 로고    scopus 로고
    • Automated refinement for protein crystallography
    • Lamzin, V. S., and Wilson, K. S. (1997) Automated refinement for protein crystallography, Methods Enzymol. 277, 269-305.
    • (1997) Methods Enzymol. , vol.277 , pp. 269-305
    • Lamzin, V.S.1    Wilson, K.S.2
  • 23
    • 0000036869 scopus 로고    scopus 로고
    • Simulation of activation free energies in molecular systems
    • Neria, E., Fischer, S., and Karplus, M. (1996) Simulation of activation free energies in molecular systems, J. Chem. Phys. 105, 1902-1921.
    • (1996) J. Chem. Phys. , vol.105 , pp. 1902-1921
    • Neria, E.1    Fischer, S.2    Karplus, M.3
  • 24
    • 0027794972 scopus 로고
    • Targeted molecular dynamics simulation of conformational change: Application to the T-R transition in insulin
    • Schlitter, J., Engels, M., Kruger, P., Jacoby, E. U., and Wollmer, A. (1993) Targeted molecular dynamics simulation of conformational change: application to the T-R transition in insulin, Mol. Simul. 10, 291-308.
    • (1993) Mol. Simul. , vol.10 , pp. 291-308
    • Schlitter, J.1    Engels, M.2    Kruger, P.3    Jacoby, E.U.4    Wollmer, A.5
  • 25
    • 33645858780 scopus 로고
    • Transferable intermolecular potential functions for water, alcohols, and ethers. Application to liquid water
    • Jorgensen, W. L. (1981) Transferable intermolecular potential functions for water, alcohols, and ethers. Application to liquid water, J. Am. Chem. Soc. 103, 335-340.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 335-340
    • Jorgensen, W.L.1
  • 26
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., Ciccotti, G., and Berendsen, H. J. C. (1977) Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes, J. Comput. Phys. 23, 327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 27
    • 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. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 29
    • 0017402592 scopus 로고
    • The primary structure of Leu, Ile and Val (LIV)-binding protein from Escherichia coli
    • Ovchinnikov, Y. A., Aldanova, N. A., Arzamazova, N. M., and Moroz, I. N. (1977) The primary structure of Leu, Ile and Val (LIV)-binding protein from Escherichia coli, FEBS Lett. 75, 313-316.
    • (1977) FEBS Lett. , vol.75 , pp. 313-316
    • Ovchinnikov, Y.A.1    Aldanova, N.A.2    Arzamazova, N.M.3    Moroz, I.N.4
  • 30
    • 0022260273 scopus 로고
    • The complete nucleotide sequences of the Escherichia coli LIV-BP and LS-BP genes. Implications for the mechanism of high-affinity branched-chain amino acid transport
    • Landick, R., and Oxender, D. L. (1985) The complete nucleotide sequences of the Escherichia coli LIV-BP and LS-BP genes. Implications for the mechanism of high-affinity branched-chain amino acid transport, J. Biol. Chem. 260, 8257-8261.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8257-8261
    • Landick, R.1    Oxender, D.L.2
  • 31
    • 0025299887 scopus 로고
    • Occurrence and role of cis peptide bonds in protein structures
    • Steward, D. E., Sarkar, A., and Wampler, J. E. (1990) Occurrence and role of cis peptide bonds in protein structures, J. Mol. Biol. 214, 253-260.
    • (1990) J. Mol. Biol. , vol.214 , pp. 253-260
    • Steward, D.E.1    Sarkar, A.2    Wampler, J.E.3
  • 32
    • 0033584887 scopus 로고    scopus 로고
    • Cis peptide bonds in proteins: Residues involved, their conformations, interactions and locations
    • Pal, D., and Chakrabarti, P. (1999) Cis peptide bonds in proteins: Residues involved, their conformations, interactions and locations, J. Mol. Biol. 294, 271-288.
    • (1999) J. Mol. Biol. , vol.294 , pp. 271-288
    • Pal, D.1    Chakrabarti, P.2
  • 33
    • 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
  • 34
    • 0000885331 scopus 로고
    • Harmonic analysis of large systems. I. Methodology
    • Brooks, B. R., Janezcic, D., and Karplus, M. (1995) Harmonic analysis of large systems. I. Methodology, J. Comput. Chem. 16, 1522-1542.
    • (1995) J. Comput. Chem. , vol.16 , pp. 1522-1542
    • Brooks, B.R.1    Janezcic, D.2    Karplus, M.3
  • 35
    • 0022111715 scopus 로고
    • Normal modes for specific motions of macromolecules: Application to the hinge-bending mode of lysozyme
    • Brooks, B., and Karplus, M. (1985) Normal modes for specific motions of macromolecules: Application to the hinge-bending mode of lysozyme, Proc. Natl. Acad. Sci. U.S.A. 82, 4995-4999.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 4995-4999
    • Brooks, B.1    Karplus, M.2
  • 36
    • 0022419152 scopus 로고
    • Protein normal-mode dynamics: Trypsin inhibitor, crambin, ribonuclease and lysozyme
    • Levitt, M., Sander, C., and Stern, P. S. (1985) Protein normal-mode dynamics: Trypsin inhibitor, crambin, ribonuclease and lysozyme, J. Mol. Biol. 181, 423-447.
    • (1985) J. Mol. Biol. , vol.181 , pp. 423-447
    • Levitt, M.1    Sander, C.2    Stern, P.S.3
  • 37
    • 0027171026 scopus 로고
    • Leucine/isoleucine/valine-binding protein contracts upon binding of ligand
    • Olah, G. A., Trakhanov, S., Trewhella, J., and Quiocho, F. A. (1993) Leucine/isoleucine/valine-binding protein contracts upon binding of ligand, J. Biol. Chem. 268, 16241-16247.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16241-16247
    • Olah, G.A.1    Trakhanov, S.2    Trewhella, J.3    Quiocho, F.A.4
  • 38
    • 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
  • 39
  • 40
    • 0025754301 scopus 로고
    • The 2.3-Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., Lu, G. Y., and Quiocho, F. A. (1991) The 2.3-Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor 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
    • 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., and 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
  • 42
    • 0027235488 scopus 로고
    • Three-dimensional structures 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., and Kim, S. H. (1993) Three-dimensional structures 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
  • 43
    • 0029200246 scopus 로고
    • 2 Å resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor
    • Nickitenko, A. V., Trakhanov, S., and Quiocho, F. A. (1995) 2 Å resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor, Biochemistry 34, 16585-16595.
    • (1995) Biochemistry , vol.34 , pp. 16585-16595
    • Nickitenko, A.V.1    Trakhanov, S.2    Quiocho, F.A.3
  • 44
    • 0030855775 scopus 로고    scopus 로고
    • Peptide binding in OppA, the crystal structures of the periplasmic oligopeptide binding protein in the unliganded form and in complex with lysyllysine
    • Sleigh, S. H., Tame, J. R., Dodson, E. J., and Wilkinson, A. J. (1997) Peptide binding in OppA, the crystal structures of the periplasmic oligopeptide binding protein in the unliganded form and in complex with lysyllysine, Biochemistry 36, 9747-9758.
    • (1997) Biochemistry , vol.36 , pp. 9747-9758
    • Sleigh, S.H.1    Tame, J.R.2    Dodson, E.J.3    Wilkinson, A.J.4
  • 45
    • 0025000575 scopus 로고
    • High specificity of a phosphate transport protein determined by hydrogen bonds
    • Luecke, H., and Quiocho, F. A. (1990) High specificity of a phosphate transport protein determined by hydrogen bonds, Nature 347, 402-406.
    • (1990) Nature , vol.347 , pp. 402-406
    • Luecke, H.1    Quiocho, F.A.2
  • 46
    • 0029900085 scopus 로고    scopus 로고
    • Negative electrostatic surface potential of protein sites specific for anionic ligands
    • Ledvina, P. S., Yao, N., Choudhary, A., and Quiocho, F. A. (1996) Negative electrostatic surface potential of protein sites specific for anionic ligands, Proc. Natl. Acad. Sci. U.S.A 93, 6786-6791.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 6786-6791
    • Ledvina, P.S.1    Yao, N.2    Choudhary, A.3    Quiocho, F.A.4
  • 47
    • 0032562651 scopus 로고    scopus 로고
    • The structure of glutamine-binding protein complexed with glutamine at 1.94 Å resolution: Comparisons with other amino acid binding proteins
    • Sun, Y.-J., Rose, J., Wang, B.-C., and Hsiao, C.-D. (1998) The structure of glutamine-binding protein complexed with glutamine at 1.94 Å resolution: comparisons with other amino acid binding proteins, J. Mol. Biol. 278, 219-229.
    • (1998) J. Mol. Biol. , vol.278 , pp. 219-229
    • Sun, Y.-J.1    Rose, J.2    Wang, B.-C.3    Hsiao, C.-D.4
  • 48
    • 0030595368 scopus 로고    scopus 로고
    • The crystal structure of the glutamine-binding protein from Escherichia coli
    • Hsiao, C. D., Sun, Y. J., Rose, J., and Wang, B. C. (1996) The crystal structure of the glutamine-binding protein from Escherichia coli, J. Mol. Biol. 262, 225-242.
    • (1996) J. Mol. Biol. , vol.262 , pp. 225-242
    • Hsiao, C.D.1    Sun, Y.J.2    Rose, J.3    Wang, B.C.4
  • 49
    • 0346118916 scopus 로고    scopus 로고
    • Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli
    • Heddle, J., Scott, D. J., Unzai, S., Park, S. Y., and Tame, J. R. (2003) Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli, J. Biol. Chem. 278, 50322-50329.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50322-50329
    • Heddle, J.1    Scott, D.J.2    Unzai, S.3    Park, S.Y.4    Tame, J.R.5
  • 50
    • 1642365068 scopus 로고    scopus 로고
    • New advances in normal mode analysis of supermolecular complexes and applications to structural refinement
    • Ma, J. (2004) New advances in normal mode analysis of supermolecular complexes and applications to structural refinement, Curr. Protein Pept. Sci. 5, 119-123.
    • (2004) Curr. Protein Pept. Sci. , vol.5 , pp. 119-123
    • Ma, J.1
  • 51
    • 0025145011 scopus 로고
    • Progress in the identification of interaction sites on the periplasmic maltose binding protein from E. coli
    • Martineau, P., Saurin, W., Hofnung, M., Spurlino, J. C., and Quiocho, F. A. (1990) Progress in the identification of interaction sites on the periplasmic maltose binding protein from E. coli, Biochimie 72, 397-402.
    • (1990) Biochimie , vol.72 , pp. 397-402
    • Martineau, P.1    Saurin, W.2    Hofnung, M.3    Spurlino, J.C.4    Quiocho, F.A.5
  • 52
    • 0016313797 scopus 로고
    • Transport of sugars and amino acids in bacteria. XII. Substrate specificities of the branched chain amino acid-binding proteins of Escherichia coli
    • Amanuma, H., and Anraku, Y. (1974) Transport of sugars and amino acids in bacteria. XII. Substrate specificities of the branched chain amino acid-binding proteins of Escherichia coli, J. Biochem. (Tokyo) 76, 1165-1173.
    • (1974) J. Biochem. (Tokyo) , vol.76 , pp. 1165-1173
    • Amanuma, H.1    Anraku, Y.2
  • 53
    • 0021804775 scopus 로고
    • Sulphate sequestered in the sulfate-binding protein is bound solely by hydrogen bonds
    • Pflugrath, J. W., and Quiocho, F. A. (1985) Sulphate sequestered in the sulfate-binding protein is bound solely by hydrogen bonds, Nature 314, 257-260.
    • (1985) Nature , vol.314 , pp. 257-260
    • Pflugrath, J.W.1    Quiocho, F.A.2
  • 54
    • 0027488714 scopus 로고
    • Dominant role of local dipoles in stabilizing uncompensated charges on a sulfate sequestered in a periplasmic active transport protein
    • He, J. J., and Quiocho, F. A. (1993) Dominant role of local dipoles in stabilizing uncompensated charges on a sulfate sequestered in a periplasmic active transport protein, Protein Sci. 2, 1643-1647.
    • (1993) Protein Sci. , vol.2 , pp. 1643-1647
    • He, J.J.1    Quiocho, F.A.2
  • 55
    • 0038342435 scopus 로고    scopus 로고
    • Crystal structure of M. tuberculosis ABC phosphate transport receptor: Specificity and charge compensation dominated by ion-dipole interactions
    • Vyas, N. K., Vyas, M. N., and Quiocho, F. A. (2003) Crystal structure of M. tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions, Structure 11, 765-774.
    • (2003) Structure , vol.11 , pp. 765-774
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 56
    • 0037154084 scopus 로고    scopus 로고
    • Structural evidence for the dominant role of nonpolar interactions in the binding of a transport/chemonsensory receptor to its highly polar ligands
    • Duan, X., and Quiocho, F. A. (2002) Structural evidence for the dominant role of nonpolar interactions in the binding of a transport/chemonsensory receptor to its highly polar ligands, Biochemistry 41, 706-712.
    • (2002) Biochemistry , vol.41 , pp. 706-712
    • Duan, X.1    Quiocho, F.A.2
  • 57
    • 0031678068 scopus 로고    scopus 로고
    • Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: Equilibrium, kinetic, and crystallographic studies
    • Ledvina, P. S., Tsai, A. L., Wang, Z., Koehl, E., and Quiocho, F. A. (1998) Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: equilibrium, kinetic, and crystallographic studies, Protein Sci. 7, 2550-2559.
    • (1998) Protein Sci. , vol.7 , pp. 2550-2559
    • Ledvina, P.S.1    Tsai, A.L.2    Wang, Z.3    Koehl, E.4    Quiocho, F.A.5
  • 58
    • 0021062151 scopus 로고
    • Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis
    • Miller, D. M., III, 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, 13665-13672.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13665-13672
    • Miller III, D.M.1    Olson, J.S.2    Pflugrath, J.W.3    Quiocho, F.A.4
  • 59
    • 0025716317 scopus 로고
    • Atomic structures of periplasmic binding proteins and the high-affinity active transport system in bacteria
    • Quiocho, F. A. (1990) Atomic structures of periplasmic binding proteins and the high-affinity active transport system in bacteria, Philos. Trans. R. Soc. London 326, 341-351.
    • (1990) Philos. Trans. R. Soc. London , vol.326 , pp. 341-351
    • Quiocho, F.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.