메뉴 건너뛰기




Volumn 82, Issue 3, 2014, Pages 386-398

Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation

Author keywords

HisJ; Molecular dynamics; Periplasmic binding protein; Protein dynamics; Protein structure

Indexed keywords

ABC TRANSPORTER; BACTERIAL PROTEIN; HISTIDINE; PERIPLASMIC BINDING PROTEIN;

EID: 84893734804     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24396     Document Type: Article
Times cited : (11)

References (69)
  • 1
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu HC, Heppel LA. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J Biol Chem 1965;240:3685-3692.
    • (1965) J Biol Chem , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 2
    • 0014010845 scopus 로고
    • The release of enzymes by osmotic shock from Escherichia coli in exponential phase
    • Nossal NG, Heppel LA. The release of enzymes by osmotic shock from Escherichia coli in exponential phase. J Biol Chem 1966;241:3055-3062.
    • (1966) J Biol Chem , vol.241 , pp. 3055-3062
    • Nossal, N.G.1    Heppel, L.A.2
  • 3
    • 0014011710 scopus 로고
    • Amino-acid-binding protein released from Escherichia coli by osmotic shock
    • Piperno JR, Oxender DL. Amino-acid-binding protein released from Escherichia coli by osmotic shock. J Biol Chem 1966;241:5732-5734.
    • (1966) J Biol Chem , vol.241 , pp. 5732-5734
    • Piperno, J.R.1    Oxender, D.L.2
  • 4
    • 0035011106 scopus 로고    scopus 로고
    • A new family of high-affinity ABC manganese and zinc permeases
    • Claverys JP. A new family of high-affinity ABC manganese and zinc permeases. Res Microbiol 2001;152:231-243.
    • (2001) Res Microbiol , vol.152 , pp. 231-243
    • Claverys, J.P.1
  • 5
    • 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, Nishikawa K. Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history. J Mol Biol 1999;286:279-290.
    • (1999) J Mol Biol , vol.286 , pp. 279-290
    • Fukami-Kobayashi, K.1    Tateno, Y.2    Nishikawa, K.3
  • 6
    • 24744459983 scopus 로고    scopus 로고
    • Periplasmic binding proteins involved in bacterial iron uptake. In: Crosa JH, Mey AR, Payne SM, editors. Washington, D.C.: ASM Press;
    • Krewulak KD, Peacock RS, Vogel HJ. Periplasmic binding proteins involved in bacterial iron uptake. In: Crosa JH, Mey AR, Payne SM, editors. Iron transport in bacteria. Washington, D.C.: ASM Press; 2004. p 499.
    • (2004) Iron transport in bacteria , pp. 499
    • Krewulak, K.D.1    Peacock, R.S.2    Vogel, H.J.3
  • 7
    • 0032984288 scopus 로고    scopus 로고
    • Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
    • Lee YH, Deka RK, Norgard MV, Radolf JD, Hasemann CA. Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone. Nat Struct Biol 1999;6:628-633.
    • (1999) Nat Struct Biol , vol.6 , pp. 628-633
    • Lee, Y.H.1    Deka, R.K.2    Norgard, M.V.3    Radolf, J.D.4    Hasemann, C.A.5
  • 8
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes
    • Quiocho FA, Ledvina PS. Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Mol Microbiol 1996;20:17-25.
    • (1996) Mol Microbiol , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 9
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam R, Saier MH Jr. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol Rev 1993;57:320-346.
    • (1993) Microbiol Rev , vol.57 , pp. 320-346
    • Tam, R.1    Saier Jr, M.H.2
  • 10
    • 50049089034 scopus 로고    scopus 로고
    • Structural biology of bacterial iron uptake
    • Krewulak KD, Vogel HJ. Structural biology of bacterial iron uptake. Biochim Biophys Acta 2008;1778:1781-1804.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1781-1804
    • Krewulak, K.D.1    Vogel, H.J.2
  • 11
    • 78651359481 scopus 로고    scopus 로고
    • A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport
    • Chu BC, Vogel HJ. A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport. Biol Chem 2011;392:39-52.
    • (2011) Biol Chem , vol.392 , pp. 39-52
    • Chu, B.C.1    Vogel, H.J.2
  • 13
    • 33544461370 scopus 로고    scopus 로고
    • The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors
    • Felder CB, Graul RC, Lee AY, Merkle HP, Sadee W. The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors. AAPS Pharm Sci 1999;1:E2.
    • (1999) AAPS Pharm Sci , vol.1
    • Felder, C.B.1    Graul, R.C.2    Lee, A.Y.3    Merkle, H.P.4    Sadee, W.5
  • 14
    • 0022555851 scopus 로고
    • Bacterial periplasmic transport systems: structure, mechanism, and evolution
    • Ames GF. Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu Rev Biochem 1986;55:397-425.
    • (1986) Annu Rev Biochem , vol.55 , pp. 397-425
    • Ames, G.F.1
  • 15
    • 0015501422 scopus 로고
    • The histidine-binding protein J is a component of histidine transport, Identification of its structural gene
    • Ames GF, Lever JE. The histidine-binding protein J is a component of histidine transport. Identification of its structural gene, hisJ. J Biol Chem 1972;247:4309-4316.
    • (1972) his J. J Biol Chem , vol.247 , pp. 4309-4316
    • Ames, G.F.1    Lever, J.E.2
  • 16
    • 0015423515 scopus 로고
    • Quantitative assay of the binding of small molecules to protein: comparison of dialysis and membrane filter assays
    • Lever JE. Quantitative assay of the binding of small molecules to protein: comparison of dialysis and membrane filter assays. Anal Biochem 1972;50:73-83.
    • (1972) Anal Biochem , vol.50 , pp. 73-83
    • Lever, J.E.1
  • 17
    • 0028067178 scopus 로고
    • The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins
    • Oh BH, Kang CH, De Bondt H, Kim SH, Nikaido K, Joshi AK, Ames GF. The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins. J Biol Chem 1994;269:4135-4143.
    • (1994) J Biol Chem , vol.269 , pp. 4135-4143
    • Oh, B.H.1    Kang, C.H.2    De Bondt, H.3    Kim, S.H.4    Nikaido, K.5    Joshi, A.K.6    Ames, G.F.7
  • 18
    • 0029787272 scopus 로고    scopus 로고
    • Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity
    • Wolf A, Lee KC, Kirsch JF, Ames GF. Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity. J Biol Chem 1996;271:21243-21250.
    • (1996) J Biol Chem , vol.271 , pp. 21243-21250
    • Wolf, A.1    Lee, K.C.2    Kirsch, J.F.3    Ames, G.F.4
  • 19
    • 0037134502 scopus 로고    scopus 로고
    • X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin
    • Clarke TE, Braun V, Winkelmann G, Tari LW, Vogel HJ. X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin. J Biol Chem 2002;277:13966-13972.
    • (2002) J Biol Chem , vol.277 , pp. 13966-13972
    • Clarke, T.E.1    Braun, V.2    Winkelmann, G.3    Tari, L.W.4    Vogel, H.J.5
  • 20
    • 0034044581 scopus 로고    scopus 로고
    • Studies and syntheses of siderophores, microbial iron chelators, and analogs as potential drug delivery agents
    • Roosenberg JM, Lin YM, Lu Y, Miller MJ. Studies and syntheses of siderophores, microbial iron chelators, and analogs as potential drug delivery agents. Curr Med Chem 2000;7:159-197.
    • (2000) Curr Med Chem , vol.7 , pp. 159-197
    • Roosenberg, J.M.1    Lin, Y.M.2    Lu, Y.3    Miller, M.J.4
  • 21
    • 79953899942 scopus 로고    scopus 로고
    • Allosteric modulation of family C G-protein-coupled receptors: from molecular insights to therapeutic perspectives
    • Urwyler S. Allosteric modulation of family C G-protein-coupled receptors: from molecular insights to therapeutic perspectives. Pharmacol Rev 2011;63:59-126.
    • (2011) Pharmacol Rev , vol.63 , pp. 59-126
    • Urwyler, S.1
  • 22
    • 0038752617 scopus 로고    scopus 로고
    • Computational design of receptor and sensor proteins with novel functions
    • Looger LL, Dwyer MA, Smith JJ, Hellinga HW. Computational design of receptor and sensor proteins with novel functions. Nature 2003;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
  • 23
    • 0028106033 scopus 로고
    • The histidine-binding protein undergoes conformational changes in the absence of ligand as analyzed with conformation-specific monoclonal antibodies
    • Wolf A, Shaw EW, Nikaido K, Ames GF. The histidine-binding protein undergoes conformational changes in the absence of ligand as analyzed with conformation-specific monoclonal antibodies. J Biol Chem 1994;269:23051-23058.
    • (1994) J Biol Chem , vol.269 , pp. 23051-23058
    • Wolf, A.1    Shaw, E.W.2    Nikaido, K.3    Ames, G.F.4
  • 24
    • 0028174670 scopus 로고
    • Refined 1.89-A structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins
    • Yao N, Trakhanov S, Quiocho FA. Refined 1.89-A structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins. Biochemistry 1994;33:4769-4779.
    • (1994) Biochemistry , vol.33 , pp. 4769-4779
    • Yao, N.1    Trakhanov, S.2    Quiocho, F.A.3
  • 26
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997;18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 28
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS All-Atom force field on conformational energetics and properties of organic liquids
    • Jorgensen WL, Maxwell DS, Tirado-Rives J. Development and testing of the OPLS All-Atom force field on conformational energetics and properties of organic liquids. J Am Chem Soc 1996;118:11225-11236.
    • (1996) J Am Chem Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 29
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemcial calculations on peptides
    • Kaminski GA, Friesner RA, Tirado-Rives J, Jorgensen WL. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemcial calculations on peptides. J Phys Chem B 2001;105:6474-6487.
    • (2001) J Phys Chem B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 30
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration. In: Pullman B, editor. The Netherlands: Reidel, Dordrecht.
    • Berendsen HJ, Postma J, Van Gusteren W, Hermans J. Interaction models for water in relation to protein hydration. In: Pullman B, editor. Intermolecular forces. The Netherlands: Reidel, Dordrecht; 1981. pp 331-342.
    • (1981) Intermolecular forces , pp. 331-342
    • Berendsen, H.J.1    Postma, J.2    Van Gusteren, W.3    Hermans, J.4
  • 31
    • 0001585978 scopus 로고    scopus 로고
    • Improving efficiency of large time-scale molecular dynamics simulations of hydrogen-rich systems
    • Feenstra KA, Hess B, Berendsen HJ. Improving efficiency of large time-scale molecular dynamics simulations of hydrogen-rich systems. J Comput Chem 1999;20:786-798.
    • (1999) J Comput Chem , vol.20 , pp. 786-798
    • Feenstra, K.A.1    Hess, B.2    Berendsen, H.J.3
  • 32
    • 77950387315 scopus 로고    scopus 로고
    • Molecular dynamics simulations of beta-ketoacyl-, beta-hydroxyacyl-, and trans-2-enoyl-acyl carrier proteins of Escherichia coli
    • Chan DI, Tieleman DP, Vogel HJ. Molecular dynamics simulations of beta-ketoacyl-, beta-hydroxyacyl-, and trans-2-enoyl-acyl carrier proteins of Escherichia coli. Biochemistry 2010;49:2860-2868.
    • (2010) Biochemistry , vol.49 , pp. 2860-2868
    • Chan, D.I.1    Tieleman, D.P.2    Vogel, H.J.3
  • 33
    • 0242292035 scopus 로고    scopus 로고
    • Brute-force molecular dynamics simulations of Villin headpiece: comparison with NMR parameters
    • van der Spoel D, Lindahl B. Brute-force molecular dynamics simulations of Villin headpiece: comparison with NMR parameters. J Phys Chem B 2003;107:11178-11187.
    • (2003) J Phys Chem B , vol.107 , pp. 11178-11187
    • van der Spoel, D.1    Lindahl, B.2
  • 35
    • 33846823909 scopus 로고
    • Particle mesh Ewald-an NLog(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen LG. Particle mesh Ewald-an NLog(N) method for Ewald sums in large systems. J Chem Phys 1993;98:10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.G.3
  • 41
    • 0032802062 scopus 로고    scopus 로고
    • On the convergence of the conformational coordinates basis set obtained by the essential dynamics analysis of proteins' molecular dynamics simulations
    • Amadei A, Ceruso MA, Di Nola A. On the convergence of the conformational coordinates basis set obtained by the essential dynamics analysis of proteins' molecular dynamics simulations. Proteins 1999;36:419-424.
    • (1999) Proteins , vol.36 , pp. 419-424
    • Amadei, A.1    Ceruso, M.A.2    Di Nola, A.3
  • 43
    • 84893796385 scopus 로고    scopus 로고
    • Schrodinger, LLC. The PyMOL molecular graphics system, version 1.3r1. The PyMOL Molecular Graphics System
    • Schrodinger, LLC. The PyMOL molecular graphics system, version 1.3r1. The PyMOL Molecular Graphics System, 2010.
    • (2010)
  • 44
    • 79958772218 scopus 로고    scopus 로고
    • Conformational dynamics of L-lysine, L-arginine, L-ornithine binding protein reveals ligand-dependent plasticity
    • Silva DA, Dominguez-Ramirez L, Rojo-Dominguez A, Sosa-Peinado A. Conformational dynamics of L-lysine, L-arginine, L-ornithine binding protein reveals ligand-dependent plasticity. Proteins 2011;79:2097-2108.
    • (2011) Proteins , vol.79 , pp. 2097-2108
    • Silva, D.A.1    Dominguez-Ramirez, L.2    Rojo-Dominguez, A.3    Sosa-Peinado, A.4
  • 45
    • 84870658986 scopus 로고    scopus 로고
    • Carbohydrate affinity for the glucose-galactose binding protein is regulated by allosteric domain motions
    • Ortega G, Castano D, Diercks T, Millet O. Carbohydrate affinity for the glucose-galactose binding protein is regulated by allosteric domain motions. J Am Chem Soc 2012;134:19869-19876.
    • (2012) J Am Chem Soc , vol.134 , pp. 19869-19876
    • Ortega, G.1    Castano, D.2    Diercks, T.3    Millet, O.4
  • 46
    • 82455201507 scopus 로고    scopus 로고
    • Solution NMR studies of periplasmic binding proteins and their interaction partners
    • Pistolesi S, Tjandra N, Bermejo GA. Solution NMR studies of periplasmic binding proteins and their interaction partners. BioMol Concepts 2011;2:53-64.
    • (2011) BioMol Concepts , vol.2 , pp. 53-64
    • Pistolesi, S.1    Tjandra, N.2    Bermejo, G.A.3
  • 47
    • 77749286394 scopus 로고    scopus 로고
    • Ligand-free open-closed transitions of periplasmic binding proteins: the case of glutamine-binding protein
    • Bermejo GA, Strub MP, Ho C, Tjandra N. Ligand-free open-closed transitions of periplasmic binding proteins: the case of glutamine-binding protein. Biochemistry 2010;49:1893-1902.
    • (2010) Biochemistry , vol.49 , pp. 1893-1902
    • Bermejo, G.A.1    Strub, M.P.2    Ho, C.3    Tjandra, N.4
  • 48
    • 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, Berendsen HJ. Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins 1998;30:144-154.
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 49
    • 0029022325 scopus 로고
    • Structure/function analysis of the periplasmic histidine-binding protein. Mutations decreasing ligand binding alter the properties of the conformational change and of the closed form
    • Wolf A, Shaw EW, Oh BH, De Bondt H, Joshi AK, Ames GF. Structure/function analysis of the periplasmic histidine-binding protein. Mutations decreasing ligand binding alter the properties of the conformational change and of the closed form. J Biol Chem 1995;270:16097-16106.
    • (1995) J Biol Chem , vol.270 , pp. 16097-16106
    • Wolf, A.1    Shaw, E.W.2    Oh, B.H.3    De Bondt, H.4    Joshi, A.K.5    Ames, G.F.6
  • 50
    • 27744606438 scopus 로고    scopus 로고
    • A salt-bridge motif involved in ligand binding and large-scale domain motions of the maltose-binding protein
    • Stockner T, Vogel HJ, Tieleman DP. A salt-bridge motif involved in ligand binding and large-scale domain motions of the maltose-binding protein. Biophys J 2005;89:3362-3371.
    • (2005) Biophys J , vol.89 , pp. 3362-3371
    • Stockner, T.1    Vogel, H.J.2    Tieleman, D.P.3
  • 51
    • 35548976322 scopus 로고    scopus 로고
    • Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
    • Tang C, Schwieters CD, Clore GM. Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR. Nature 2007;449:1078-1082.
    • (2007) Nature , vol.449 , pp. 1078-1082
    • Tang, C.1    Schwieters, C.D.2    Clore, G.M.3
  • 53
    • 0029900085 scopus 로고    scopus 로고
    • Negative electrostatic surface potential of protein sites specific for anionic ligands
    • Ledvina PS, Yao N, Choudhary A, Quiocho FA. Negative electrostatic surface potential of protein sites specific for anionic ligands. Proc Natl Acad Sci U S A 1996;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
  • 54
    • 0025000575 scopus 로고
    • High specificity of a phosphate transport protein determined by hydrogen bonds
    • Luecke H, Quiocho FA. High specificity of a phosphate transport protein determined by hydrogen bonds. Nature 1990;347:402-406.
    • (1990) Nature , vol.347 , pp. 402-406
    • Luecke, H.1    Quiocho, F.A.2
  • 55
    • 0032511137 scopus 로고    scopus 로고
    • Multiple open forms of ribose-binding protein trace the path of its conformational change
    • Bjorkman AJ, Mowbray SL. Multiple open forms of ribose-binding protein trace the path of its conformational change. J Mol Biol 1998;279:651-664.
    • (1998) J Mol Biol , vol.279 , pp. 651-664
    • Bjorkman, A.J.1    Mowbray, S.L.2
  • 56
    • 0027235488 scopus 로고
    • Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand
    • Oh BH, Pandit J, Kang CH, Nikaido K, Gokcen S, Ames GF, Kim SH. Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand. J Biol Chem 1993;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.6    Kim, S.H.7
  • 57
    • 0037671391 scopus 로고    scopus 로고
    • Interdomain dynamics and ligand binding: molecular dynamics simulations of glutamine binding protein
    • Pang A, Arinaminpathy Y, Sansom MSP, Biggin PC. Interdomain dynamics and ligand binding: molecular dynamics simulations of glutamine binding protein. FEBS Lett 2003;550:168-174.
    • (2003) FEBS Lett , vol.550 , pp. 168-174
    • Pang, A.1    Arinaminpathy, Y.2    Sansom, M.S.P.3    Biggin, P.C.4
  • 58
    • 35048866000 scopus 로고    scopus 로고
    • Characterization of protein conformational states by normal-mode frequencies
    • Hall BA, Kaye SL, Pang A, Perera R, Biggin PC. Characterization of protein conformational states by normal-mode frequencies. J Am Chem Soc 2007;129:11394-11401.
    • (2007) J Am Chem Soc , vol.129 , pp. 11394-11401
    • Hall, B.A.1    Kaye, S.L.2    Pang, A.3    Perera, R.4    Biggin, P.C.5
  • 59
    • 79958136745 scopus 로고    scopus 로고
    • A role for both conformational selection and induced fit in ligand binding by the LAO protein
    • Silva DA, Bowman GR, Sosa-Peinado A, Huang X. A role for both conformational selection and induced fit in ligand binding by the LAO protein. PLoS Comput Biol 2011;7:e1002054.
    • (2011) PLoS Comput Biol , vol.7
    • Silva, D.A.1    Bowman, G.R.2    Sosa-Peinado, A.3    Huang, X.4
  • 60
    • 53249084550 scopus 로고    scopus 로고
    • Molecular dynamics simulations of ligand-induced backbone conformational changes in the binding site of the periplasmic lysine-, arginine-, ornithine-binding protein
    • Yang AY, Mancera RL. Molecular dynamics simulations of ligand-induced backbone conformational changes in the binding site of the periplasmic lysine-, arginine-, ornithine-binding protein. J Comput Aided Mol Des 2008;22:799-814.
    • (2008) J Comput Aided Mol Des , vol.22 , pp. 799-814
    • Yang, A.Y.1    Mancera, R.L.2
  • 61
    • 28644451763 scopus 로고    scopus 로고
    • Comparative molecular dynamics-similar folds and similar motions?
    • Pang A, Arinaminpathy Y, Sansom MS, Biggin PC. Comparative molecular dynamics-similar folds and similar motions? Proteins 2005;61:809-822.
    • (2005) Proteins , vol.61 , pp. 809-822
    • Pang, A.1    Arinaminpathy, Y.2    Sansom, M.S.3    Biggin, P.C.4
  • 62
    • 0033936376 scopus 로고    scopus 로고
    • Thermodynamics and dynamics of histidine-binding protein, the water-soluble receptor of histidine permease. Implications for the transport of high and low affinity ligands
    • Kreimer DI, Malak H, Lakowicz JR, Trakhanov S, Villar E, Shnyrov VL. Thermodynamics and dynamics of histidine-binding protein, the water-soluble receptor of histidine permease. Implications for the transport of high and low affinity ligands. Eur J Biochem 2000;267:4242-4252.
    • (2000) Eur J Biochem , vol.267 , pp. 4242-4252
    • Kreimer, D.I.1    Malak, H.2    Lakowicz, J.R.3    Trakhanov, S.4    Villar, E.5    Shnyrov, V.L.6
  • 63
    • 0027171026 scopus 로고
    • Leucine/isoleucine/valine-binding protein contracts upon binding of ligand
    • Olah GA, Trakhanov S, Trewhella J, Quiocho FA. Leucine/isoleucine/valine-binding protein contracts upon binding of ligand. J Biol Chem 1993;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
  • 64
    • 0028002085 scopus 로고
    • The 1.9 A x-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium
    • Flocco MM, Mowbray SL. The 1.9 A x-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium. J Biol Chem 1994;269:8931-8936.
    • (1994) J Biol Chem , vol.269 , pp. 8931-8936
    • Flocco, M.M.1    Mowbray, S.L.2
  • 65
    • 70349823496 scopus 로고    scopus 로고
    • Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation
    • Oswald C, Smits SH, Hoing M, Bremer E, Schmitt L. Structural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformation. Biol Chem 2009;390:1163-1170.
    • (2009) Biol Chem , vol.390 , pp. 1163-1170
    • Oswald, C.1    Smits, S.H.2    Hoing, M.3    Bremer, E.4    Schmitt, L.5
  • 66
    • 57749122030 scopus 로고    scopus 로고
    • Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states
    • Oswald C, Smits SH, Hoing M, Sohn-Bosser L, Dupont L, Le Rudulier D, Schmitt L, Bremer E. Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states. J Biol Chem 2008;283:32848-32859.
    • (2008) J Biol Chem , vol.283 , pp. 32848-32859
    • Oswald, C.1    Smits, S.H.2    Hoing, M.3    Sohn-Bosser, L.4    Dupont, L.5    Le Rudulier, D.6    Schmitt, L.7    Bremer, E.8
  • 67
    • 0024604620 scopus 로고
    • Reconstitution of the histidine periplasmic transport system in membrane vesicles. Energy coupling and interaction between the binding protein and the membrane complex
    • Prossnitz E, Gee A, Ames GF. Reconstitution of the histidine periplasmic transport system in membrane vesicles. Energy coupling and interaction between the binding protein and the membrane complex. J Biol Chem 1989;264:5006-5014.
    • (1989) J Biol Chem , vol.264 , pp. 5006-5014
    • Prossnitz, E.1    Gee, A.2    Ames, G.F.3
  • 68
    • 17544365410 scopus 로고    scopus 로고
    • Liganded and unliganded receptors interact with equal affinity with the membrane complex of periplasmic permeases, a subfamily of traffic ATPases
    • Ames GF, Liu CE, Joshi AK, Nikaido K. Liganded and unliganded receptors interact with equal affinity with the membrane complex of periplasmic permeases, a subfamily of traffic ATPases. J Biol Chem 1996;271:14264-14270.
    • (1996) J Biol Chem , vol.271 , pp. 14264-14270
    • Ames, G.F.1    Liu, C.E.2    Joshi, A.K.3    Nikaido, K.4
  • 69
    • 0033534452 scopus 로고    scopus 로고
    • Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex. Effect of different ligands and consequences for the mechanism of action
    • Liu CE, Liu PQ, Wolf A, Lin E, Ames GF. Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex. Effect of different ligands and consequences for the mechanism of action. J Biol Chem 1999;274:739-747.
    • (1999) J Biol Chem , vol.274 , pp. 739-747
    • Liu, C.E.1    Liu, P.Q.2    Wolf, A.3    Lin, E.4    Ames, G.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.