메뉴 건너뛰기




Volumn 99, Issue 7, 2010, Pages 2309-2317

Large domain fluctuations on 50-ns timescale enable catalytic activity in phosphoglycerate kinase

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77958157527     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.08.017     Document Type: Article
Times cited : (57)

References (44)
  • 2
    • 0028331255 scopus 로고
    • Normal-mode analysis of protein dynamics
    • Case, D. A. 1994. Normal-mode analysis of protein dynamics. Curr. Opin. Struct. Biol. 4:285-290.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 285-290
    • Case, D.A.1
  • 3
    • 0031853060 scopus 로고    scopus 로고
    • Protein dynamics from NMR
    • Kay, L. E. 1998. Protein dynamics from NMR. Nat. Struct. Biol. 5 (Suppl ):513-517.
    • (1998) Nat. Struct. Biol. , vol.5 , Issue.SUPPL. , pp. 513-517
    • Kay, L.E.1
  • 5
    • 0000539364 scopus 로고
    • Glucose-induced conformational change in yeast hexokinase
    • Bennett, Jr., W. S., and T. A. Steitz. 1978. Glucose-induced conformational change in yeast hexokinase. Proc. Natl. Acad. Sci. USA. 75:4848-4852.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4848-4852
    • Bennett Jr., W.S.1    Steitz, T.A.2
  • 6
    • 36849048228 scopus 로고    scopus 로고
    • Intrinsic motions along an enzymatic reaction trajectory
    • Henzler-Wildman, K. A., V. Thai, D. Kern. 2007. Intrinsic motions along an enzymatic reaction trajectory. Nature. 450:838-844.
    • (2007) Nature , vol.450 , pp. 838-844
    • Henzler-Wildman, K.A.1    Thai, V.2    Kern, D.3
  • 7
    • 53449084212 scopus 로고    scopus 로고
    • Direct observation of correlated interdomain motion in alcohol dehydrogenase
    • Biehl, R., B. Hoffmann, D. Richter. 2008. Direct observation of correlated interdomain motion in alcohol dehydrogenase. Phys. Rev. Lett. 101:138102.
    • (2008) Phys. Rev. Lett. , vol.101 , pp. 138102
    • Biehl, R.1    Hoffmann, B.2    Richter, D.3
  • 8
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., A. M. Lesk, andC. Chothia. 1994. Structural mechanisms for domain movements in proteins. Biochemistry. 33:6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 9
    • 0022117176 scopus 로고
    • Segmental flexibility in pig immunoglobulin G studied by neutron spin-echo technique
    • Alpert, Y., L. Cser, Y. M. Ostanevich. 1985. Segmental flexibility in pig immunoglobulin G studied by neutron spin-echo technique. Biopolymers. 24:1769-1784.
    • (1985) Biopolymers , vol.24 , pp. 1769-1784
    • Alpert, Y.1    Cser, L.2    Ostanevich, Y.M.3
  • 10
    • 29144461924 scopus 로고    scopus 로고
    • Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy
    • Bu, Z., R. Biehl, D. J. Callaway. 2005. Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy. Proc. Natl. Acad. Sci. USA. 102:17646-17651.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17646-17651
    • Bu, Z.1    Biehl, R.2    Callaway, D.J.3
  • 11
    • 77956928348 scopus 로고
    • 3rd ed. P. D. Boyer, editor. Academic Press, New York
    • Scope, R. K. 1973. The Enzymes, 3rd ed. P. D. Boyer, editor. Academic Press, New York. 335-351.
    • (1973) The Enzymes , pp. 335-351
    • Scope, R.K.1
  • 12
    • 0015970128 scopus 로고
    • Structure of yeast phosphoglycerate kinase
    • Bryant, T. N., H. C. Watson, and P. L. Wendell. 1974. Structure of yeast phosphoglycerate kinase. Nature. 247:14-17.
    • (1974) Nature , vol.247 , pp. 14-17
    • Bryant, T.N.1    Watson, H.C.2    Wendell, P.L.3
  • 13
    • 0018803381 scopus 로고
    • Sequence, structure and activity of phosphoglycerate kinase: A possible hinge-bending enzyme
    • Banks, R. D., C. C. F. Blake, A. W. Phillips. 1979. Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme. Nature. 279:773-777.
    • (1979) Nature , vol.279 , pp. 773-777
    • Banks, R.D.1    Blake, C.C.F.2    Phillips, A.W.3
  • 14
    • 0031573453 scopus 로고    scopus 로고
    • Closed structure ofphosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability
    • Auerbach, G., R. Huber, U. Jacob. 1997. Closed structure ofphosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. Structure. 5:1475-1483.
    • (1997) Structure , vol.5 , pp. 1475-1483
    • Auerbach, G.1    Huber, R.2    Jacob, U.3
  • 15
    • 0026536746 scopus 로고
    • Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate
    • Harlos, K., M. Vas, and C. F. Blake. 1992. Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate. Proteins. 12:133-144.
    • (1992) Proteins , vol.12 , pp. 133-144
    • Harlos, K.1    Vas, M.2    Blake, C.F.3
  • 16
    • 0031030767 scopus 로고    scopus 로고
    • Synergistic effects of substrate-induced changes in phosphoglycerate kinase activation
    • Bernstein, B. E., P. A. Michels, and W. G. Hol. 1997. Synergistic effects of substrate-induced changes in phosphoglycerate kinase activation. Nature. 385:275-278.
    • (1997) Nature , vol.385 , pp. 275-278
    • Bernstein, B.E.1    Michels, P.A.2    Hol, W.G.3
  • 17
    • 0030553275 scopus 로고    scopus 로고
    • Low frequency motions in phosphoglycerate kinase: A normal mode analysis
    • Guilbert, C., F. Pecorari, L. Mouawad. 1996. Low frequency motions in phosphoglycerate kinase: a normal mode analysis. Chem. Phys. 204:327-336.
    • (1996) Chem. Phys. , vol.204 , pp. 327-336
    • Guilbert, C.1    Pecorari, F.2    Mouawad, L.3
  • 18
    • 0024635350 scopus 로고
    • Correlation between enzyme activity and hinge-bending domain displacement in 3-phosphoglycerate kinase
    • Sinev, M. A., O. I. Razgulyaev, O. B. Ptitsyn. 1989. Correlation between enzyme activity and hinge-bending domain displacement in 3-phosphoglycerate kinase. Eur. J. Biochem. 180:61-66.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 61-66
    • Sinev, M.A.1    Razgulyaev, O.I.2    Ptitsyn, O.B.3
  • 19
    • 0018606116 scopus 로고
    • Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase
    • Pickover, C. A., D. B. McKay, T. A. Steitz. 1979. Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase. J. Biol. Chem. 254:11323-11329.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11323-11329
    • Pickover, C.A.1    McKay, D.B.2    Steitz, T.A.3
  • 20
    • 0028080301 scopus 로고
    • Conformational changes in yeast phosphoglycerate kinase upon substrate binding
    • Henderson, S. J., E. H. Serpersu, G. J. Bunick. 1994. Conformational changes in yeast phosphoglycerate kinase upon substrate binding. Biophys. Chem. 53:95-104.
    • (1994) Biophys. Chem. , vol.53 , pp. 95-104
    • Henderson, S.J.1    Serpersu, E.H.2    Bunick, G.J.3
  • 21
    • 0027337984 scopus 로고
    • Configurational distribution of denatured phosphoglycerate kinase
    • Calmettes, P., B. Roux, J. C. Smith. 1993. Configurational distribution of denatured phosphoglycerate kinase. J. Mol. Biol. 231:840-848.
    • (1993) J. Mol. Biol. , vol.231 , pp. 840-848
    • Calmettes, P.1    Roux, B.2    Smith, J.C.3
  • 22
    • 0027074883 scopus 로고
    • Domain motions in phosphoglycerate kinase: Determination of interdomain distance distributions by site-specific labeling and time-resolved fluorescence energy transfer
    • Haran, G., E. Haas, M. T. Mas. 1992. Domain motions in phosphoglycerate kinase: Determination of interdomain distance distributions by site-specific labeling and time-resolved fluorescence energy transfer. Proc. Natl. Acad. Sci. USA. 89:11764-11768.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11764-11768
    • Haran, G.1    Haas, E.2    Mas, M.T.3
  • 23
    • 33745024278 scopus 로고    scopus 로고
    • Symmetry, form, and shape: Guiding principles for robustness in macromolecular machines
    • Tama, F., and C. L. Brooks. 2006. Symmetry, form, and shape: guiding principles for robustness in macromolecular machines. Annu. Rev. Biophys. Biomol. Struct. 35:115-133.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 115-133
    • Tama, F.1    Brooks, C.L.2
  • 24
    • 14844286108 scopus 로고    scopus 로고
    • Usefulness and limitations of normal mode analysis in modeling dynamics of biomolecular complexes
    • Ma, J. 2005. Usefulness and limitations of normal mode analysis in modeling dynamics of biomolecular complexes. Structure. 13: 373-380.
    • (2005) Structure , vol.13 , pp. 373-380
    • Ma, J.1
  • 25
    • 0000197372 scopus 로고    scopus 로고
    • Large amplitude elastic motions in proteins from a single-parameter, atomic analysis
    • Tirion, M. M. 1996. Large amplitude elastic motions in proteins from a single-parameter, atomic analysis. Phys. Rev. Lett. 77:1905-1908.
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 1905-1908
    • Tirion, M.M.1
  • 27
    • 84933693670 scopus 로고
    • An analytic structure factor formacroion solutions
    • Hayter, J. B., and J. Penfold. 1981. An analytic structure factor formacroion solutions. Mol. Phys. 42:109-118.
    • (1981) Mol. Phys. , vol.42 , pp. 109-118
    • Hayter, J.B.1    Penfold, J.2
  • 28
    • 3242875210 scopus 로고    scopus 로고
    • ElNemo: A normal mode web server for protein movement analysis and the generation of templates for molecular replacement
    • Suhre, K., and Y. H. Sanejouand. 2004. ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Res. 32(Web Server issue): W610-W614.
    • (2004) Nucleic Acids Res. , vol.32 , Issue.WEB SERVER ISSUE
    • Suhre, K.1    Sanejouand, Y.H.2
  • 29
    • 36149052898 scopus 로고
    • The dynamics of interacting Brownian particles
    • Pusey, P. N. 1975. The dynamics of interacting Brownian particles. J. Phys. A. 8:1433-1440.
    • (1975) J. Phys. A. , vol.8 , pp. 1433-1440
    • Pusey, P.N.1
  • 30
    • 36749113106 scopus 로고
    • Correlations for interacting Brownian particles
    • Ackerson, B. J. 1976. Correlations for interacting Brownian particles. J. Chem. Phys. 64:242-246.
    • (1976) J. Chem. Phys. , vol.64 , pp. 242-246
    • Ackerson, B.J.1
  • 31
    • 5544266284 scopus 로고
    • Interpretation of the intermediate scattering function at short times
    • Ackerson, B. J., P. N. Pusey, and R. J. A. Tough. 1981. Interpretation of the intermediate scattering function at short times. J. Chem. Phys. 76:1279-1282.
    • (1981) J. Chem. Phys. , vol.76 , pp. 1279-1282
    • Ackerson, B.J.1    Pusey, P.N.2    Tough, R.J.A.3
  • 32
    • 0030188212 scopus 로고    scopus 로고
    • On the dynamics and structure of charge-stabilized suspensions
    • Nägele, G. 1996. On the dynamics and structure of charge-stabilized suspensions. Phys. Rep. 272:215-372.
    • (1996) Phys. Rep. , vol.272 , pp. 215-372
    • Nägele, G.1
  • 33
    • 0020176542 scopus 로고
    • A constrained regularization method for inverting data represented by linear algebraic or integral equations
    • Provencher, S. W. 1982. A constrained regularization method for inverting data represented by linear algebraic or integral equations. Comput. Phys. Commun. 27:213-227.
    • (1982) Comput. Phys. Commun. , vol.27 , pp. 213-227
    • Provencher, S.W.1
  • 34
    • 0018447571 scopus 로고
    • Some measurements of the shape and hydrodynamic properties of yeast phosphoglycerate kinase (E.C.2.7.2.3)
    • Smith, J., and S. P. Spragg. 1979. Some measurements of the shape and hydrodynamic properties of yeast phosphoglycerate kinase (E.C.2.7.2.3). Biophys. Chem. 9:215-221.
    • (1979) Biophys. Chem. , vol.9 , pp. 215-221
    • Smith, J.1    Spragg, S.P.2
  • 35
    • 40849119960 scopus 로고    scopus 로고
    • Short-time transport properties in dense suspensions: From neutral to charge-stabilized colloidal spheres
    • Banchio, A. J., and G. Nagele. 2008. Short-time transport properties in dense suspensions: from neutral to charge-stabilized colloidal spheres. J. Chem. Phys. 128:104903.
    • (2008) J. Chem. Phys. , vol.128 , pp. 104903
    • Banchio, A.J.1    Nagele, G.2
  • 37
    • 0011333023 scopus 로고
    • The effects ofhydrodynamic interactions on translational and rotational relaxation
    • Montgomery, J. A., and B. J. Berne. 1977. The effects ofhydrodynamic interactions on translational and rotational relaxation. J. Chem. Phys. 67:4589-4596.
    • (1977) J. Chem. Phys. , vol.67 , pp. 4589-4596
    • Montgomery, J.A.1    Berne, B.J.2
  • 38
    • 0016891076 scopus 로고
    • Quasielastic scattering by dilute polymer solutions
    • Akcasu, Z., and H. Gurol. 1976. Quasielastic scattering by dilute polymer solutions. J. Polym. Sci., B Polym. Phys. Ed. 14:1-10.
    • (1976) J. Polym. Sci., B Polym. Phys. Ed. , vol.14 , pp. 1-10
    • Akcasu, Z.1    Gurol, H.2
  • 39
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • García De La Torre, J., M. L. Huertas, and B. Carrasco. 2000. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78:719-730.
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • De La Torre, J.G.1    Huertas, M.L.2    Carrasco, B.3
  • 40
    • 0001347793 scopus 로고
    • Effect of rotational diffusion on quasielastic light scattering from fractal colloid aggregates
    • Lindsay, H. M., R. Klein, P. Meakin. 1988. Effect of rotational diffusion on quasielastic light scattering from fractal colloid aggregates. Phys. Rev. A. 38:2614-2626.
    • (1988) Phys. Rev. A. , vol.38 , pp. 2614-2626
    • Lindsay, H.M.1    Klein, R.2    Meakin, P.3
  • 41
    • 0000619829 scopus 로고
    • Dynamics of neutron scattering molecules
    • Zemach, A. C., and R. J. Glauber. 1956. Dynamics of neutron scattering molecules. Phys. Rev. 101:118-129.
    • (1956) Phys. Rev. , vol.101 , pp. 118-129
    • Zemach, A.C.1    Glauber, R.J.2
  • 42
    • 0029946037 scopus 로고    scopus 로고
    • Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate
    • McPhillips, T. M., B. T. Hsu, D. C. Rees. 1996. Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate. Biochemistry. 35: 4118-4127.
    • (1996) Biochemistry , vol.35 , pp. 4118-4127
    • McPhillips, T.M.1    Hsu, B.T.2    Rees, D.C.3
  • 43
    • 0001060193 scopus 로고    scopus 로고
    • Site-directed mutagenesis of proline 204 in the 'hinge' region of yeast phosphoglycerate kinase
    • McHarg, J., S. M. Kelly, J. A. Littlechild. 1999. Site-directed mutagenesis of proline 204 in the 'hinge' region of yeast phosphoglycerate kinase. Eur. J. Biochem. 259:939-945.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 939-945
    • McHarg, J.1    Kelly, S.M.2    Littlechild, J.A.3
  • 44
    • 25444475247 scopus 로고    scopus 로고
    • Reaction barrier heights from an exact-exchange-based density-functional correlation model
    • Dickinson, R. M., and A. D. Becke. 2005. Reaction barrier heights from an exact-exchange-based density-functional correlation model. J. Chem. Phys. 123, 111101-111101-3.
    • (2005) J. Chem. Phys. , vol.123 , pp. 1111010-1111013
    • Dickinson, R.M.1    Becke, A.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.