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Volumn 340, Issue 2, 2004, Pages 345-372

A normal mode analysis of structural plasticity in the biomolecular motor F1-ATPase

Author keywords

ABNR, adapted basis Newton Rhapson; BMD, biased molecular dynamics; BNM, block normal mode; conformational transition; F1 ATPase; normal mode analysis; RMSF, root mean square fluctuations; structural flexibility

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 2942511344     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.04.044     Document Type: Article
Times cited : (144)

References (63)
  • 1
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Boyer P. The ATP synthase - a splendid molecular machine. Annu. Rev. Biochem. 66:1997;717-749
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.1
  • 2
    • 0032544312 scopus 로고    scopus 로고
    • ATP synthesis by rotary catalysis (nobel lecture)
    • Walker J.E. ATP synthesis by rotary catalysis (nobel lecture). Angew. Chem., Int. Ed. Engl. 37:1998;2309-2319
    • (1998) Angew. Chem., Int. Ed. Engl. , vol.37 , pp. 2309-2319
    • Walker, J.E.1
  • 3
    • 0034737965 scopus 로고    scopus 로고
    • ATP synthase: What we know about ATP hydrolysis and what we do not know about ATP synthesis
    • Weber J., Senior A.E. ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis. Biochim. Biophys. Acta. 1458:2000;300-309
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 300-309
    • Weber, J.1    Senior, A.E.2
  • 5
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase - Some probabilities and possibilities
    • Boyer P.D. The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta. 1140:1993;215-250
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 8
    • 0035838982 scopus 로고    scopus 로고
    • 1-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotatory catalysis
    • 1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotatory catalysis. Cell. 106:2001;331-341
    • (2001) Cell , vol.106 , pp. 331-341
    • Menz, R.I.1    Walker, J.E.2    Leslie, A.G.W.3
  • 9
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi V.K., Girvin M.E. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature. 402:1999;263
    • (1999) Nature , vol.402 , pp. 263
    • Rastogi, V.K.1    Girvin, M.E.2
  • 12
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • Junge W., Lill H., Engelbrecht S. ATP synthase: an electrochemical transducer with rotatory mechanics. Trends Biochem. Sci. 22:1997;420-423
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 13
    • 0034866072 scopus 로고    scopus 로고
    • Viscoelastic dynamics of actin filaments coupled to rotatory F-ATPase: Angular torque profile of the enzyme
    • Panke O., Cherepanov D.A., Gumbiowski K., Engelbrecht S., Junge W. Viscoelastic dynamics of actin filaments coupled to rotatory F-ATPase: angular torque profile of the enzyme. Biophys. J. 81:2001;1220-1233
    • (2001) Biophys. J. , vol.81 , pp. 1220-1233
    • Panke, O.1    Cherepanov, D.A.2    Gumbiowski, K.3    Engelbrecht, S.4    Junge, W.5
  • 14
    • 0034859197 scopus 로고    scopus 로고
    • Viscoelastic dynamics of actin filaments coupled to rotatory F-ATPase: Curvature as an indicator of the torque
    • Cherepanov D.A., Junge W. Viscoelastic dynamics of actin filaments coupled to rotatory F-ATPase: curvature as an indicator of the torque. Biophys. J. 81:2001;1234-1244
    • (2001) Biophys. J. , vol.81 , pp. 1234-1244
    • Cherepanov, D.A.1    Junge, W.2
  • 15
    • 0032547899 scopus 로고    scopus 로고
    • 1 motor of ATP synthase
    • 1 motor of ATP synthase. Nature. 396:1997;279-282
    • (1997) Nature , vol.396 , pp. 279-282
    • Wang, H.1    Oster, G.2
  • 18
    • 2942511282 scopus 로고
    • C.P. Lee, C. Schatz, L. Ernster, & P.D. Boyer. Waltham: Addison-Wesley
    • Lee C.P., Schatz C., Ernster L., Boyer P.D. Membrane Bioenergetics. 1979;Addison-Wesley, Waltham
    • (1979) Membrane Bioenergetics
  • 23
    • 0032555216 scopus 로고    scopus 로고
    • The allosteric mechanism of the chaperonin GroEL: A dynamic analysis
    • Ma J., Karplus M. The allosteric mechanism of the chaperonin GroEL: a dynamic analysis. Proc. Natl Acad. Sci. USA. 95:1998;8502
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8502
    • Ma, J.1    Karplus, M.2
  • 24
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama F., Sanejouand Y. Conformational change of proteins arising from normal mode calculations. Protein Eng. 14:2001;1
    • (2001) Protein Eng. , vol.14 , pp. 1
    • Tama, F.1    Sanejouand, Y.2
  • 27
    • 0032932341 scopus 로고    scopus 로고
    • Tertiary and quaternary conformational changes in aspartate transcarbamylase: A normal mode study
    • Thomas A., Hinsen K., Field M.J., Perahia D. Tertiary and quaternary conformational changes in aspartate transcarbamylase: a normal mode study. Proteins: Struct. Funct. Genet. 34:1999;96
    • (1999) Proteins: Struct. Funct. Genet. , vol.34 , pp. 96
    • Thomas, A.1    Hinsen, K.2    Field, M.J.3    Perahia, D.4
  • 29
    • 0034738090 scopus 로고    scopus 로고
    • Reverse engineering a protein: The mechanochemistry of ATP synthase
    • Oster G., Wang H. Reverse engineering a protein: the mechanochemistry of ATP synthase. Biochim. Biophys. Acta. 1458:2000;482-510
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 482-510
    • Oster, G.1    Wang, H.2
  • 33
    • 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
    • Haywards S., Kitao A., Berendsen H.J.C. Model-free methods of analyzing domain motions in proteins from simulation: a comparison of normal mode analysis and molecular dynamics simulation of lysozyme. Proteins: Struct. Funct. Genet. 27:1997;425
    • (1997) Proteins: Struct. Funct. Genet. , vol.27 , pp. 425
    • Haywards, S.1    Kitao, A.2    Berendsen, H.J.C.3
  • 34
    • 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., Wollmer A. Targeted molecular dynamics simulation of conformational change-application to the t-r transition in insulin. Mol. Simul. 10:1993;291-308
    • (1993) Mol. Simul. , vol.10 , pp. 291-308
    • Schlitter, J.1    Engels, M.2    Kruger, P.3    Jacoby, E.4    Wollmer, A.5
  • 35
    • 0032568695 scopus 로고    scopus 로고
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120°steps
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120°steps. Cell. 93:1998;1117-1124
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinoshita, K.3    Yoshida, M.4
  • 38
    • 0022111715 scopus 로고
    • Normal modes for specific motions of macromolecules: Applications to the hinge-bending mode of lysozyme
    • Brooks B.R., Karplus M. Normal modes for specific motions of macromolecules: applications to the hinge-bending mode of lysozyme. Proc. Natl Acad. Sci. USA. 82:1985;4995
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 4995
    • Brooks, B.R.1    Karplus, M.2
  • 39
    • 0023035967 scopus 로고
    • Interdomian motion in liver alcohol dehydrogenase: Structural and energetic analysis of the hinge bending mode
    • Colonna-Cesari F., Perahia D., Karplus M., Ecklund H., Bränden C.I., Tapia O. Interdomian motion in liver alcohol dehydrogenase: structural and energetic analysis of the hinge bending mode. J. Biol. Chem. 261:1986;15273
    • (1986) J. Biol. Chem. , vol.261 , pp. 15273
    • Colonna-Cesari, F.1    Perahia, D.2    Karplus, M.3    Ecklund, H.4    Bränden, C.I.5    Tapia, O.6
  • 40
    • 0025015392 scopus 로고
    • Anatomy of a protein conformational change: Hinged lid motion of the triosephosphate isomerase loop
    • Joseph D., Petsko G.A., Karplus M. Anatomy of a protein conformational change: hinged lid motion of the triosephosphate isomerase loop. Science. 249:1990;1425
    • (1990) Science , vol.249 , pp. 1425
    • Joseph, D.1    Petsko, G.A.2    Karplus, M.3
  • 42
    • 1842584700 scopus 로고    scopus 로고
    • Mechanical coupling in myosin: A theoretical analysis of ATP hydrolysis with molecular dynamics and combined QM/MM reaction path calculations
    • Li, G. & Cui, Q. (2004). Mechanical coupling in myosin: a theoretical analysis of ATP hydrolysis with molecular dynamics and combined QM/MM reaction path calculations. J. Phys. Chem. B, 108, 3342-3357.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3342-3357
    • Li, G.1    Cui, Q.2
  • 43
    • 0000885331 scopus 로고
    • Harmonic analysis of large systems. I. Methodology
    • Brooks B.R., Janeic D., Karplus M. Harmonic analysis of large systems. I. Methodology. J. Comput. Chem. 16:1995;1522-1542
    • (1995) J. Comput. Chem. , vol.16 , pp. 1522-1542
    • Brooks, B.R.1    Janeic, D.2    Karplus, M.3
  • 45
    • 0000036869 scopus 로고    scopus 로고
    • Simulation of activation free energies in molecular systems
    • Neria E., Fisher S., Karplus M. Simulation of activation free energies in molecular systems. J. Chem. Phys. 105:1997;1902-1921
    • (1997) J. Chem. Phys. , vol.105 , pp. 1902-1921
    • Neria, E.1    Fisher, S.2    Karplus, M.3
  • 46
  • 48
    • 0001031179 scopus 로고
    • Proteins: A theoretical perspective of dynamics, structure and thermodynamics
    • Brooks C.L. III, Karplus M., Pettitt B.M. Proteins: a theoretical perspective of dynamics, structure and thermodynamics. Advan. Chem. Phys. 71:1988;1-249
    • (1988) Advan. Chem. Phys. , vol.71 , pp. 1-249
    • Brooks III, C.L.1    Karplus, M.2    Pettitt, B.M.3
  • 49
    • 0031561292 scopus 로고    scopus 로고
    • Continuum treatment of long-range interactions in free energy calculations, application to protein-ligand binding
    • Simonson T., Archontis G., Karplus M. Continuum treatment of long-range interactions in free energy calculations, application to protein-ligand binding. J. Phys. Chem. B. 41:1997;8347-8360
    • (1997) J. Phys. Chem. B , vol.41 , pp. 8347-8360
    • Simonson, T.1    Archontis, G.2    Karplus, M.3
  • 53
    • 0000197372 scopus 로고    scopus 로고
    • Large amplitude elastic motions in proteins from a single-parameter atomic analysis
    • Tirion M.M. Large amplitude elastic motions in proteins from a single-parameter atomic analysis. Phys. Rev. Letters. 77:1996;1905-1908
    • (1996) Phys. Rev. Letters , vol.77 , pp. 1905-1908
    • Tirion, M.M.1
  • 54
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • Bahar I., Atilgan R., Erman B. Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Fold. Des. 2:1997;173-181
    • (1997) Fold. Des. , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, R.2    Erman, B.3
  • 55
    • 84986450150 scopus 로고
    • Principles for a direct SCF approach to LCAO-MO ab initio calculations
    • Almlof J., Faegri K., Korsell K. Principles for a direct SCF approach to LCAO-MO ab initio calculations. J. Comput. Chem. 3:1982;385
    • (1982) J. Comput. Chem. , vol.3 , pp. 385
    • Almlof, J.1    Faegri, K.2    Korsell, K.3
  • 56
    • 0000094594 scopus 로고
    • An iterative method for the solution of the eigenvalue problem of linear differential and integral operators
    • Lanczos C. An iterative method for the solution of the eigenvalue problem of linear differential and integral operators. J. Res. Natl Bur. Stand. 45:1950;255
    • (1950) J. Res. Natl Bur. Stand. , vol.45 , pp. 255
    • Lanczos, C.1
  • 60
    • 0032975875 scopus 로고    scopus 로고
    • A study of vibrational relaxation of B-state carbon monoxide in the heme pocket of photolyzed carboxymyoglobin
    • Sagnella D.E., Straub J.E. A study of vibrational relaxation of B-state carbon monoxide in the heme pocket of photolyzed carboxymyoglobin. Biophys. J. 77:1999;70
    • (1999) Biophys. J. , vol.77 , pp. 70
    • Sagnella, D.E.1    Straub, J.E.2
  • 61
    • 0029560322 scopus 로고
    • Hinge-bending motion in citrate synthase arising from normal mode calculations
    • Marques O., Sanejouand Y. Hinge-bending motion in citrate synthase arising from normal mode calculations. Proteins: Struct. Funct. Genet. 23:1995;557
    • (1995) Proteins: Struct. Funct. Genet. , vol.23 , pp. 557
    • Marques, O.1    Sanejouand, Y.2
  • 62
    • 0030700726 scopus 로고    scopus 로고
    • Ligand induced conformational changes in ras p21: A normal mode and energy minimization study
    • Ma J., Karplus M. Ligand induced conformational changes in ras p21: a normal mode and energy minimization study. J. Mol. Biol. 274:1997;114
    • (1997) J. Mol. Biol. , vol.274 , pp. 114
    • Ma, J.1    Karplus, M.2


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