메뉴 건너뛰기




Volumn 45, Issue 44, 2006, Pages 13284-13292

Opening and closing motions in the periplasmic vitamin B12 binding protein BtuF

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; CONFORMATIONS; CRYSTAL STRUCTURE; ESCHERICHIA COLI; MOLECULAR DYNAMICS; VITAMINS;

EID: 33750736650     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061280j     Document Type: Article
Times cited : (53)

References (65)
  • 1
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R., and Saier, M. H., Jr. (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 Jr., M.H.2
  • 2
    • 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
  • 3
    • 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
  • 4
    • 4143115810 scopus 로고    scopus 로고
    • Periplasmic binding proteins: A versatile superfamily for protein engineering
    • Dwyer, M. A., and Hellinga, H. W. (2004) Periplasmic binding proteins: A versatile superfamily for protein engineering, Curr. Opin. Struct. Biol. 14, 495-504.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 495-504
    • Dwyer, M.A.1    Hellinga, H.W.2
  • 5
    • 0031004715 scopus 로고    scopus 로고
    • Chaperone properties of the bacterial periplasmic substrate-binding proteins
    • Richarme, G., and Caldas, T. D. (1997) Chaperone properties of the bacterial periplasmic substrate-binding proteins, J. Biol. Chem. 272, 15607-15612.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15607-15612
    • Richarme, G.1    Caldas, T.D.2
  • 6
    • 0343395846 scopus 로고    scopus 로고
    • ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12
    • Koster, W. (2001) ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12, Res. Microbiol. 152, 291-301.
    • (2001) Res. Microbiol. , vol.152 , pp. 291-301
    • Koster, W.1
  • 7
    • 0034255851 scopus 로고    scopus 로고
    • Diversity of transport mechanisms: Common structural principles
    • Driessen, A. J., Rosen, B. P., and Konings, W. N. (2000) Diversity of transport mechanisms: Common structural principles, Trends Biochem. Sci. 25, 397-401.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 397-401
    • Driessen, A.J.1    Rosen, B.P.2    Konings, W.N.3
  • 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
    • 0019888766 scopus 로고
    • The radius of gyration of L-arabinose-binding protein decreases upon binding of ligand
    • Newcomer, M. E., Lewis, B. A., and Quiocho, F. A. (1981) The radius of gyration of L-arabinose-binding protein decreases upon binding of ligand, J. Biol. Chem. 256, 13218-13222.
    • (1981) J. Biol. Chem. , vol.256 , pp. 13218-13222
    • Newcomer, M.E.1    Lewis, B.A.2    Quiocho, F.A.3
  • 10
    • 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., and Kim, S. M. (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.6    Kim, S.M.7
  • 11
    • 0035352440 scopus 로고    scopus 로고
    • Structural biology of bacterial iron uptake systems
    • Clarke, T. E., Tari, L. W., and Vogel, H. J. (2000) Structural biology of bacterial iron uptake systems, Curr. Top. Med. Chem. 1, 7-30.
    • (2000) Curr. Top. Med. Chem. , vol.1 , pp. 7-30
    • Clarke, T.E.1    Tari, L.W.2    Vogel, H.J.3
  • 12
    • 0019888716 scopus 로고
    • L-Arabinose-binding protein-sugar complex at 2.4 Å resolution. Stereochemistry and evidence for a structural change
    • Newcomer, M. E., Gilliland, G. L., and Quiocho, F. A. (1981) L-Arabinose-binding protein-sugar complex at 2.4 Å resolution. Stereochemistry and evidence for a structural change, J. Biol. Chem. 256, 13213-13217.
    • (1981) J. Biol. Chem. , vol.256 , pp. 13213-13217
    • Newcomer, M.E.1    Gilliland, G.L.2    Quiocho, F.A.3
  • 13
    • 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
  • 14
    • 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
  • 15
    • 0037168666 scopus 로고    scopus 로고
    • The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter
    • Borths, E. L., Locher, K. P., Lee, A. T., and Rees, D. C. (2002) The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter, Proc. Natl. Acad. Sci. U.S.A. 99, 16642-16647.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16642-16647
    • Borths, E.L.1    Locher, K.P.2    Lee, A.T.3    Rees, D.C.4
  • 16
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the 2 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 2 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
  • 17
    • 0032984288 scopus 로고    scopus 로고
    • Treponema pallidium TroA is a periplasmic zinc-binding protein with a helical backbone
    • Lee, Y. H., Deka, R. K., Norgard, M. V., Radolf, J. D., and Hasemann, C. A. (1999) Treponema pallidium TroA is a periplasmic zinc-binding protein with a helical backbone, Nat. Struct. Biol. 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
  • 18
    • 0036209769 scopus 로고    scopus 로고
    • The crystal structure of Zn(II)-free Treponema pallidium TroA, a periplasmic metal-binding protein, reveals a closed conformation
    • Lee, Y. H., Dorwart, M. R., Hazlett, K. R., Deka, R. K., Norgard, M. V., Radolf, J. D., and Hasemann, C. A. (2002) The crystal structure of Zn(II)-free Treponema pallidium TroA, a periplasmic metal-binding protein, reveals a closed conformation, J. Bacteriol. 184, 2300-2304.
    • (2002) J. Bacteriol. , vol.184 , pp. 2300-2304
    • Lee, Y.H.1    Dorwart, M.R.2    Hazlett, K.R.3    Deka, R.K.4    Norgard, M.V.5    Radolf, J.D.6    Hasemann, C.A.7
  • 19
    • 0032534754 scopus 로고    scopus 로고
    • The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein
    • Lawrence, M. C., Pilling, P. A., Epa, V. C., Berry, A. M. Ogunniyi, A. D., and Paton, J. C. (1998) The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein, Structure 6, 1553-1561.
    • (1998) Structure , vol.6 , pp. 1553-1561
    • Lawrence, M.C.1    Pilling, P.A.2    Epa, V.C.3    Berry, A.M.4    Ogunniyi, A.D.5    Paton, J.C.6
  • 20
    • 0034127329 scopus 로고    scopus 로고
    • The structure of the ferric siderophore binding protein FhuD complexed with gallichrome
    • Clarke, T. E., Ku, S. Y., Dougan, D. R., Vogel, H. J., and Tari, L. W. (2000) The structure of the ferric siderophore binding protein FhuD complexed with gallichrome, Nat. Struct. Biol. 7, 287-291.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 287-291
    • Clarke, T.E.1    Ku, S.Y.2    Dougan, D.R.3    Vogel, H.J.4    Tari, L.W.5
  • 22
    • 0037424465 scopus 로고    scopus 로고
    • Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding
    • Karpowich, N. K., Huang, H. H., Smith, P. C., and Hunt, J. F. (2003) Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding, J. Biol. Chem. 278, 8429-8434.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8429-8434
    • Karpowich, N.K.1    Huang, H.H.2    Smith, P.C.3    Hunt, J.F.4
  • 24
    • 0242670022 scopus 로고    scopus 로고
    • Substrate-induced transmembrane signaling in the cobalamin transporter BtuB
    • Chimento, D. P., Mohanty, A. K., Kadner, R. J., and Wiener, M. C. (2003) Substrate-induced transmembrane signaling in the cobalamin transporter BtuB, Nat. Struct. Biol. 10, 394-401.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 394-401
    • Chimento, D.P.1    Mohanty, A.K.2    Kadner, R.J.3    Wiener, M.C.4
  • 25
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., Lee, A. T., and Rees, D. C. (2002) The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism, Science 296, 1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 26
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson, A. L., and Chen, J. (2004) ATP-binding cassette transporters in bacteria, Annu. Rev. Biochem. 73, 241-268.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 27
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang, G., and Roth, C. B. (2001) Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters, Science 293, 1793-1800.
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 28
    • 0038799725 scopus 로고    scopus 로고
    • Structure of MsbA from Vibrio cholera: A multidrug resistance ABC transporter homolog in a closed conformation
    • Chang, G. (2003) Structure of MsbA from Vibrio cholera: A multidrug resistance ABC transporter homolog in a closed conformation, J. Mol. Biol. 330, 419-430.
    • (2003) J. Mol. Biol. , vol.330 , pp. 419-430
    • Chang, G.1
  • 29
    • 18644363550 scopus 로고    scopus 로고
    • Structure of the ABC transporter MsbA in complex with ADP-vanadate and lipopolysaccharide
    • Reyes, C. L., and Chang, G. (2005) Structure of the ABC transporter MsbA in complex with ADP-vanadate and lipopolysaccharide, Science 308, 1028-1031.
    • (2005) Science , vol.308 , pp. 1028-1031
    • Reyes, C.L.1    Chang, G.2
  • 30
    • 1942532335 scopus 로고    scopus 로고
    • ABC transporter architecture and mechanism: Implications from the crystal structures of BtuCD and BtuF
    • Locher, K. P., and Borths, E. (2004) ABC transporter architecture and mechanism: Implications from the crystal structures of BtuCD and BtuF, FEBS Lett. 564, 264-268.
    • (2004) FEBS Lett. , vol.564 , pp. 264-268
    • Locher, K.P.1    Borths, E.2
  • 31
    • 28944442871 scopus 로고    scopus 로고
    • In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B-12 uptake
    • Borths, E. L., Poolman, B., Hvorup, R. N., Locher, K. P., and Rees, D. C. (2005) In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B-12 uptake, Biochemistry 44, 16301-16309.
    • (2005) Biochemistry , vol.44 , pp. 16301-16309
    • Borths, E.L.1    Poolman, B.2    Hvorup, R.N.3    Locher, K.P.4    Rees, D.C.5
  • 32
    • 0031910020 scopus 로고    scopus 로고
    • Locally accessible conformations of proteins: Multiple molecular dynamics simulations of crambin
    • Caves, L. S., Evanseck, J. D., and Karplus, M. (1998) Locally accessible conformations of proteins: Multiple molecular dynamics simulations of crambin, Protein Sci. 7, 649-666.
    • (1998) Protein Sci. , vol.7 , pp. 649-666
    • Caves, L.S.1    Evanseck, J.D.2    Karplus, M.3
  • 33
    • 0034739054 scopus 로고    scopus 로고
    • Multicopy molecular dynamics simulations suggest how to reconcile crystallographic and product formation data for camphor enantiomers bound to cytochrome P-450cam
    • Das, B., Helms, V., Lounnas, V., and Wade, R. C. (2000) Multicopy molecular dynamics simulations suggest how to reconcile crystallographic and product formation data for camphor enantiomers bound to cytochrome P-450cam, J. Inorg. Biochem. 81, 121-131.
    • (2000) J. Inorg. Biochem. , vol.81 , pp. 121-131
    • Das, B.1    Helms, V.2    Lounnas, V.3    Wade, R.C.4
  • 34
    • 0037671391 scopus 로고    scopus 로고
    • Interdomain dynamics and ligand binding: Molecular dynamics simulations of glutamine binding protein
    • Pang, A., Arinaminpathy, Y., Sansom, M. S. P., and Biggin, P. C. (2003) Interdomain dynamics and ligand binding: Molecular dynamics simulations of glutamine binding protein, FEBS Lett. 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
  • 35
    • 0036154304 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the ligand-binding domain of the ionotropic glutamate receptor GluR2
    • Arinaminpathy, Y., Sansom, M. S., and Biggin, P. C. (2002) Molecular dynamics simulations of the ligand-binding domain of the ionotropic glutamate receptor GluR2, Biophys. J. 82, 676-683.
    • (2002) Biophys. J. , vol.82 , pp. 676-683
    • Arinaminpathy, Y.1    Sansom, M.S.2    Biggin, P.C.3
  • 36
    • 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, H. J., and Tieleman, D. P. (2005) A salt-bridge motif involved in ligand binding and large-scale domain motions of the maltose-binding protein, Biophys. J. 89, 3362-3371.
    • (2005) Biophys. J. , vol.89 , pp. 3362-3371
    • Stockner, T.1    Vogel, H.J.2    Tieleman, D.P.3
  • 37
    • 24744441871 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the periplasmic ferric-hydroxamate binding protein FhuD
    • Krewulak, K. D., Shepherd, C. M., and Vogel, H. J. (2005) Molecular dynamics simulations of the periplasmic ferric-hydroxamate binding protein FhuD, BioMetals 18, 375-386.
    • (2005) BioMetals , vol.18 , pp. 375-386
    • Krewulak, K.D.1    Shepherd, C.M.2    Vogel, H.J.3
  • 38
    • 23344454719 scopus 로고    scopus 로고
    • Refinement of docked protein-ligand and protein-DNA structures using low-frequency normal mode amplitude optimization
    • Lindahl, E., and Delarue, M. (2005) Refinement of docked protein-ligand and protein-DNA structures using low-frequency normal mode amplitude optimization, Nucleic Acids Res. 33, 4496-4506.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4496-4506
    • Lindahl, E.1    Delarue, M.2
  • 39
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama, F., and Sanejouand, Y. H. (2001) Conformational change of proteins arising from normal mode calculations, Protein Eng. 14, 1-6.
    • (2001) Protein Eng. , vol.14 , pp. 1-6
    • Tama, F.1    Sanejouand, Y.H.2
  • 40
    • 0043238084 scopus 로고    scopus 로고
    • Dynamical properties of the MscL of Escherichia coli: A normal-mode analysis
    • Valadie, H., Lacapere, J. J., Sanejouand, Y. H., and Etchebest, C. (2003) Dynamical properties of the MscL of Escherichia coli: A normal-mode analysis, J. Mol. Biol. 332, 657-674.
    • (2003) J. Mol. Biol. , vol.332 , pp. 657-674
    • Valadie, H.1    Lacapere, J.J.2    Sanejouand, Y.H.3    Etchebest, C.4
  • 41
    • 0037436340 scopus 로고    scopus 로고
    • Mega-Dalton biomolecular motion captured from electron microscopy reconstructions
    • Chacon, P., Tama, F., and Wriggers, W. (2003) Mega-Dalton biomolecular motion captured from electron microscopy reconstructions, J. Mol. Biol. 326, 485-492.
    • (2003) J. Mol. Biol. , vol.326 , pp. 485-492
    • Chacon, P.1    Tama, F.2    Wriggers, W.3
  • 42
    • 0042424707 scopus 로고    scopus 로고
    • Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy
    • Tama, F., Valle, M., Frank, J., and Brooks, C. L., III (2003) Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy, Proc. Natl. Acad. Sci. U.S.A. 100, 9319-9323.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9319-9323
    • Tama, F.1    Valle, M.2    Frank, J.3    Brooks III, C.L.4
  • 43
    • 0029633168 scopus 로고
    • Gromacs: A message-passing parallel molecular-dynamics implementation
    • Berendsen, H. J. C., Vanderspoel, D., and Vandrunen, R. (1995) Gromacs: A Message-Passing Parallel Molecular-Dynamics Implementation, Comput. Phys. Commun. 91, 43-56.
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    Vanderspoel, D.2    Vandrunen, R.3
  • 44
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., Hess, B., and van der Spoel, D. (2001) GROMACS 3.0: A package for molecular simulation and trajectory analysis, J. Mol. Model. 7, 306-317.
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 45
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • (Pullman, B., Ed.). Reidel, Dordrecht, The Netherlands
    • Berendsen, H. J. C., Postma, J. P. M., Vangunsteren, W. F., and Hermans, J. (1981) Interaction models for water in relation to protein hydration, in Intermolecular Forces (Pullman, B., Ed.) pp 331-342. Reidel, Dordrecht, The Netherlands.
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Vangunsteren, W.F.3    Hermans, J.4
  • 47
    • 33846823909 scopus 로고
    • Particle mesh ewald: An N.Log(N) method for ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle Mesh Ewald: An N.Log(N) Method for Ewald Sums in Large Systems, J. Chem. Phys. 98, 10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 49
    • 0035849162 scopus 로고    scopus 로고
    • Parameters for the AMBER force field for the molecular mechanics modeling of the cobalt corrinoids
    • Marques, H. M., Ngoma, B., Egan, T. J., and Brown, K. L. (2001) Parameters for the AMBER force field for the molecular mechanics modeling of the cobalt corrinoids, J. Mol. Struct. 561, 71-91.
    • (2001) J. Mol. Struct. , vol.561 , pp. 71-91
    • Marques, H.M.1    Ngoma, B.2    Egan, T.J.3    Brown, K.L.4
  • 50
    • 0343799500 scopus 로고
    • A molecular mechanics force-field for the cobalt corrinoids
    • Marques, H. M., and Brown, K. L. (1995) A Molecular Mechanics Force-Field for the Cobalt Corrinoids, THEOCHEM 340, 97-124.
    • (1995) THEOCHEM , vol.340 , pp. 97-124
    • Marques, H.M.1    Brown, K.L.2
  • 52
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. 3. The role of exact exchange
    • Becke, A. D. (1993) Density-Functional Thermochemistry. 3. The Role of Exact Exchange, J. Chem. Phys. 98, 5648-5652.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 53
    • 0345491105 scopus 로고
    • Development of the colle-salvetti correlation-energy formula into a functional of the electron-density
    • Lee, C. T., Yang, W. T., and Parr, R. G. (1988) Development of the Colle-Salvetti Correlation-Energy Formula into a Functional of the Electron-Density, Phys. Rev. B 37, 785-789.
    • (1988) Phys. Rev. B , vol.37 , pp. 785-789
    • Lee, C.T.1    Yang, W.T.2    Parr, R.G.3
  • 54
    • 33745770836 scopus 로고
    • Abinitio effective core potentials for molecular calculations: Potentials for the transition-metal atoms Sc to Hg
    • Hay, P. J., and Wadt, W. R. (1985) Abinitio Effective Core Potentials for Molecular Calculations: Potentials for the Transition-Metal Atoms Sc to Hg, J. Chem. Phys. 82, 270-283.
    • (1985) J. Chem. Phys. , vol.82 , pp. 270-283
    • Hay, P.J.1    Wadt, W.R.2
  • 56
    • 0030888546 scopus 로고    scopus 로고
    • Model-free methods of analyzing domain motions in proteins from simulation: A comparison of normal mode analysis and molecular dynamics simulation of lysozyme
    • Hayward, S., Kitao, A., and Berendsen, H. J. (1997) Model-free methods of analyzing domain motions in proteins from simulation: A comparison of normal mode analysis and molecular dynamics simulation of lysozyme, Proteins 27, 425-437.
    • (1997) Proteins , vol.27 , pp. 425-437
    • Hayward, S.1    Kitao, A.2    Berendsen, H.J.3
  • 57
    • 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
  • 58
    • 0036888353 scopus 로고    scopus 로고
    • Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50
    • Hayward, S., and Lee, R. A. (2002) Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50, J. Mol. Graphics Modell. 21, 181-183.
    • (2002) J. Mol. Graphics Modell. , vol.21 , pp. 181-183
    • Hayward, S.1    Lee, R.A.2
  • 59
    • 0000939821 scopus 로고    scopus 로고
    • What is the probability of a chance prediction of a protein structure with an rmsd of 6 A?
    • Reva, B. A., Finkelstein, A. V., and Skolnick, J. (1998) What is the probability of a chance prediction of a protein structure with an rmsd of 6 A? Folding Des. 3, 141-147.
    • (1998) Folding Des. , vol.3 , pp. 141-147
    • Reva, B.A.1    Finkelstein, A.V.2    Skolnick, J.3
  • 60
    • 0035888284 scopus 로고    scopus 로고
    • Universal similarity measure for comparing protein structures
    • Betancourt, M. R., and Skolnick, J. (2001) Universal similarity measure for comparing protein structures, Biopolymer 59, 305-309.
    • (2001) Biopolymer , vol.59 , pp. 305-309
    • Betancourt, M.R.1    Skolnick, J.2
  • 61
    • 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
  • 62
    • 0346749526 scopus 로고    scopus 로고
    • The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus. Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport
    • Sebulsky, M. T., Shilton, B. H., Speziali, C. D., and Heinrichs, D. E. (2003) The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus. Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport, J. Biol. Chem. 278, 49890-49900.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49890-49900
    • Sebulsky, M.T.1    Shilton, B.H.2    Speziali, C.D.3    Heinrichs, D.E.4
  • 63
    • 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
  • 64
    • 3142619074 scopus 로고    scopus 로고
    • Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport
    • Austermuhle, M. I., Hall, J. A., Klug, C. S., and Davidson, A. L. (2004) Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport, J. Biol. Chem. 279, 28243-28250.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28243-28250
    • Austermuhle, M.I.1    Hall, J.A.2    Klug, C.S.3    Davidson, A.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.