Large Domain Fluctuations on 50-ns Timescale Enable Catalytic Activity in Phosphoglycerate Kinase
Large-scale domain motions of enzymes are often essential for their biological function. Phosphoglycerate kinase has a wide open domain structure with a hinge near the active center between the two domains. Applying neutron spin echo spectroscopy and small-angle neutron scattering we have investigat...
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Published in | Biophysical journal Vol. 99; no. 7; pp. 2309 - 2317 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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06.10.2010
Biophysical Society The Biophysical Society |
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Abstract | Large-scale domain motions of enzymes are often essential for their biological function. Phosphoglycerate kinase has a wide open domain structure with a hinge near the active center between the two domains. Applying neutron spin echo spectroscopy and small-angle neutron scattering we have investigated the internal domain dynamics. Structural analysis reveals that the holoprotein in solution seems to be more compact compared to the crystal structure but would not allow the functionally important phosphoryl transfer between the substrates if the protein were static. Brownian large-scale domain fluctuation dynamics on a timescale of 50 ns was revealed by neutron spin echo spectroscopy. The dynamics observed was compared to the displacement patterns of low-frequency normal modes. The displacements along the normal-mode coordinates describe our experimental results reasonably well. In particular, the domain movements facilitate a close encounter of the key residues in the active center to build the active configuration. The observed dynamics shows that the protein has the flexibility to allow fluctuations and displacements that seem to enable the function of the protein. Moreover, the presence of the substrates increases the rigidity, which is deduced from a faster dynamics with smaller amplitude. |
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AbstractList | Large-scale domain motions of enzymes are often essential for their biological function. Phosphoglycerate kinase has a wide open domain structure with a hinge near the active center between the two domains. Applying neutron spin echo spectroscopy and small-angle neutron scattering we have investigated the internal domain dynamics. Structural analysis reveals that the holoprotein in solution seems to be more compact compared to the crystal structure but would not allow the functionally important phosphoryl transfer between the substrates if the protein were static. Brownian large-scale domain fluctuation dynamics on a timescale of 50 ns was revealed by neutron spin echo spectroscopy. The dynamics observed was compared to the displacement patterns of low-frequency normal modes. The displacements along the normal-mode coordinates describe our experimental results reasonably well. In particular, the domain movements facilitate a close encounter of the key residues in the active center to build the active configuration. The observed dynamics shows that the protein has the flexibility to allow fluctuations and displacements that seem to enable the function of the protein. Moreover, the presence of the substrates increases the rigidity, which is deduced from a faster dynamics with smaller amplitude. Large-scale domain motions of enzymes are often essential for their biological function. Phosphoglycerate kinase has a wide open domain structure with a hinge near the active center between the two domains. Applying neutron spin echo spectroscopy and small-angle neutron scattering we have investigated the internal domain dynamics. Structural analysis reveals that the holoprotein in solution seems to be more compact compared to the crystal structure but would not allow the functionally important phosphoryl transfer between the substrates if the protein were static. Brownian large-scale domain fluctuation dynamics on a timescale of 50 ns was revealed by neutron spin echo spectroscopy. The dynamics observed was compared to the displacement patterns of low-frequency normal modes. The displacements along the normal-mode coordinates describe our experimental results reasonably well. In particular, the domain movements facilitate a close encounter of the key residues in the active center to build the active configuration. The observed dynamics shows that the protein has the flexibility to allow fluctuations and displacements that seem to enable the function of the protein. Moreover, the presence of the substrates increases the rigidity, which is deduced from a faster dynamics with smaller amplitude. [PUBLICATION ABSTRACT] |
Author | Biehl, R. Monkenbusch, M. Radulescu, A. Inoue, R. Richter, D. Rosenkranz, T. Farago, B. Fitter, J. |
AuthorAffiliation | Institut für Festköperforschung, Forschungszentrum Jülich, Jülich, Germany Institut Laue Langevin, Grenoble, France Jülich Center of Neutron Science, Forschungszentrum Jülich, Garching, Germany Institut für Strukturbiologie und Biophysik (ISB-2), Forschungszentrum Jülich, Jülich, Germany |
AuthorAffiliation_xml | – name: Institut für Festköperforschung, Forschungszentrum Jülich, Jülich, Germany – name: Institut für Strukturbiologie und Biophysik (ISB-2), Forschungszentrum Jülich, Jülich, Germany – name: Institut Laue Langevin, Grenoble, France – name: Jülich Center of Neutron Science, Forschungszentrum Jülich, Garching, Germany |
Author_xml | – sequence: 1 givenname: R. surname: Inoue fullname: Inoue, R. organization: Institut für Festköperforschung, Forschungszentrum Jülich, Jülich, Germany – sequence: 2 givenname: R. surname: Biehl fullname: Biehl, R. email: ra.biehl@fz-juelich.de organization: Institut für Festköperforschung, Forschungszentrum Jülich, Jülich, Germany – sequence: 3 givenname: T. surname: Rosenkranz fullname: Rosenkranz, T. organization: Institut für Strukturbiologie und Biophysik (ISB-2), Forschungszentrum Jülich, Jülich, Germany – sequence: 4 givenname: J. surname: Fitter fullname: Fitter, J. organization: Institut für Strukturbiologie und Biophysik (ISB-2), Forschungszentrum Jülich, Jülich, Germany – sequence: 5 givenname: M. surname: Monkenbusch fullname: Monkenbusch, M. organization: Institut für Festköperforschung, Forschungszentrum Jülich, Jülich, Germany – sequence: 6 givenname: A. surname: Radulescu fullname: Radulescu, A. organization: Jülich Center of Neutron Science, Forschungszentrum Jülich, Garching, Germany – sequence: 7 givenname: B. surname: Farago fullname: Farago, B. organization: Institut Laue Langevin, Grenoble, France – sequence: 8 givenname: D. surname: Richter fullname: Richter, D. organization: Institut für Festköperforschung, Forschungszentrum Jülich, Jülich, Germany |
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Cites_doi | 10.1073/pnas.75.10.4848 10.1016/S0168-9002(97)00956-X 10.1063/1.2868773 10.1038/247014a0 10.1103/PhysRevLett.77.1905 10.1146/annurev.biophys.35.040405.102010 10.1063/1.434619 10.1016/S0006-3495(00)76630-6 10.1093/nar/gkh368 10.1016/S0969-2126(97)00297-9 10.1038/385275a0 10.1021/bi952500o 10.1046/j.1432-1327.1999.00133.x 10.1038/279773a0 10.1016/S0021-9258(19)86488-8 10.1063/1.431957 10.1002/bip.360240908 10.1103/PhysRevLett.101.138102 10.1002/pol.1976.180140101 10.1002/prot.340120207 10.1103/PhysRev.101.118 10.1063/1.443146 10.1016/0301-4622(94)00080-8 10.1038/755 10.1021/bi00188a001 10.1016/j.str.2005.02.002 10.1016/S0959-440X(94)90321-2 10.1006/jmbi.1993.1330 10.1088/0305-4470/8/9/012 10.1073/pnas.0503388102 10.1073/pnas.89.24.11764 10.1016/0301-4622(79)85004-8 10.1016/0301-0104(95)00293-6 10.1038/nature06410 10.1016/0370-1573(95)00078-X 10.1016/0010-4655(82)90173-4 10.1103/PhysRevA.38.2614 10.1111/j.1432-1033.1989.tb14615.x 10.1080/00268978100100091 |
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References | Case (bib2) 1994; 4 Scope (bib11) 1973 Smith, Spragg (bib34) 1979; 9 Provencher (bib33) 1982; 27 Degiorgio, Piazza, Jones (bib36) 1995; 52 Tirion (bib25) 1996; 77 Bernstein, Michels, Hol (bib16) 1997; 385 Dickinson, Becke (bib44) 2005; 123 Bryant, Watson, Wendell (bib12) 1974; 247 Suhre, Sanejouand (bib28) 2004; 32 Henderson, Serpersu, Bunick (bib20) 1994; 53 Pusey (bib29) 1975; 8 McHarg, Kelly, Littlechild (bib43) 1999; 259 Hayter, Penfold (bib27) 1981; 42 Montgomery, Berne (bib37) 1977; 67 Alpert, Cser, Ostanevich (bib9) 1985; 24 Haran, Haas, Mas (bib22) 1992; 89 Ackerson, Pusey, Tough (bib31) 1981; 76 McPhillips, Hsu, Rees (bib42) 1996; 35 Calmettes, Roux, Smith (bib21) 1993; 231 Lindsay, Klein, Meakin (bib40) 1988; 38 Zemach, Glauber (bib41) 1956; 101 Akcasu, Gurol (bib38) 1976; 14 Auerbach, Huber, Jacob (bib14) 1997; 5 Guilbert, Pecorari, Mouawad (bib17) 1996; 204 Kay (bib3) 1998; 5 (bib4) 2006 Bennett, Steitz (bib5) 1978; 75 Biehl, Hoffmann, Richter (bib7) 2008; 101 García De La Torre, Huertas, Carrasco (bib39) 2000; 78 Monkenbusch, Schätzler, Richter (bib26) 1997; 399 Pickover, McKay, Steitz (bib19) 1979; 254 Sinev, Razgulyaev, Ptitsyn (bib18) 1989; 180 Henzler-Wildman, Thai, Kern (bib6) 2007; 450 McCammon, Harvey (bib1) 1987 Gerstein, Lesk, Chothia (bib8) 1994; 33 Ma (bib24) 2005; 13 Banchio, Nägele (bib35) 2008; 128 Ackerson (bib30) 1976; 64 Bu, Biehl, Callaway (bib10) 2005; 102 Harlos, Vas, Blake (bib15) 1992; 12 Nägele (bib32) 1996; 272 Tama, Brooks (bib23) 2006; 35 Banks, Blake, Phillips (bib13) 1979; 279 387770 - J Biol Chem. 1979 Nov 25;254(22):11323-9 18851497 - Phys Rev Lett. 2008 Sep 26;101(13):138102 16306270 - Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17646-51 4587639 - Nature. 1974 Jan 4;247(5435):14-7 9665181 - Nat Struct Biol. 1998 Jul;5 Suppl:513-7 9963717 - Phys Rev E Stat Phys Plasmas Fluids Relat Interdiscip Topics. 1995 Sep;52(3):2707-2717 4052583 - Biopolymers. 1985 Sep;24(9):1769-84 16689630 - Annu Rev Biophys Biomol Struct. 2006;35:115-33 9000079 - Nature. 1997 Jan 16;385(6613):275-8 10092885 - Eur J Biochem. 1999 Feb;259(3):939-45 8672447 - Biochemistry. 1996 Apr 2;35(13):4118-27 15766538 - Structure. 2005 Mar;13(3):373-80 283394 - Proc Natl Acad Sci U S A. 1978 Oct;75(10):4848-52 18026086 - Nature. 2007 Dec 6;450(7171):838-44 10063201 - Phys Rev Lett. 1996 Aug 26;77(9):1905-1908 8204609 - Biochemistry. 1994 Jun 7;33(22):6739-49 1603803 - Proteins. 1992 Feb;12(2):133-44 2707265 - Eur J Biochem. 1989 Mar 1;180(1):61-6 450128 - Nature. 1979 Jun 28;279(5716):773-7 7841334 - Biophys Chem. 1994 Dec;53(1-2):95-104 16392542 - J Chem Phys. 2005 Sep 15;123(11):111101 9900670 - Phys Rev A Gen Phys. 1988 Sep 1;38(5):2614-2626 10653785 - Biophys J. 2000 Feb;78(2):719-30 15215461 - Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W610-4 1465395 - Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11764-8 8515454 - J Mol Biol. 1993 Jun 5;231(3):840-8 378285 - Biophys Chem. 1979 Mar;9(3):215-21 18345924 - J Chem Phys. 2008 Mar 14;128(10):104903 9384563 - Structure. 1997 Nov 15;5(11):1475-83 Kay (10.1016/j.bpj.2010.08.017_bib3) 1998; 5 Hayter (10.1016/j.bpj.2010.08.017_bib27) 1981; 42 Haran (10.1016/j.bpj.2010.08.017_bib22) 1992; 89 Bennett (10.1016/j.bpj.2010.08.017_bib5) 1978; 75 Bu (10.1016/j.bpj.2010.08.017_bib10) 2005; 102 Guilbert (10.1016/j.bpj.2010.08.017_bib17) 1996; 204 Dickinson (10.1016/j.bpj.2010.08.017_bib44) 2005; 123 Ackerson (10.1016/j.bpj.2010.08.017_bib31) 1981; 76 Degiorgio (10.1016/j.bpj.2010.08.017_bib36) 1995; 52 Smith (10.1016/j.bpj.2010.08.017_bib34) 1979; 9 Bryant (10.1016/j.bpj.2010.08.017_bib12) 1974; 247 McCammon (10.1016/j.bpj.2010.08.017_bib1) 1987 Gerstein (10.1016/j.bpj.2010.08.017_bib8) 1994; 33 Lindsay (10.1016/j.bpj.2010.08.017_bib40) 1988; 38 Auerbach (10.1016/j.bpj.2010.08.017_bib14) 1997; 5 Calmettes (10.1016/j.bpj.2010.08.017_bib21) 1993; 231 Ma (10.1016/j.bpj.2010.08.017_bib24) 2005; 13 Bernstein (10.1016/j.bpj.2010.08.017_bib16) 1997; 385 Monkenbusch (10.1016/j.bpj.2010.08.017_bib26) 1997; 399 Pusey (10.1016/j.bpj.2010.08.017_bib29) 1975; 8 Banchio (10.1016/j.bpj.2010.08.017_bib35) 2008; 128 McPhillips (10.1016/j.bpj.2010.08.017_bib42) 1996; 35 Suhre (10.1016/j.bpj.2010.08.017_bib28) 2004; 32 (10.1016/j.bpj.2010.08.017_bib4) 2006 García De La Torre (10.1016/j.bpj.2010.08.017_bib39) 2000; 78 Alpert (10.1016/j.bpj.2010.08.017_bib9) 1985; 24 McHarg (10.1016/j.bpj.2010.08.017_bib43) 1999; 259 Zemach (10.1016/j.bpj.2010.08.017_bib41) 1956; 101 Tirion (10.1016/j.bpj.2010.08.017_bib25) 1996; 77 Harlos (10.1016/j.bpj.2010.08.017_bib15) 1992; 12 Provencher (10.1016/j.bpj.2010.08.017_bib33) 1982; 27 Akcasu (10.1016/j.bpj.2010.08.017_bib38) 1976; 14 Biehl (10.1016/j.bpj.2010.08.017_bib7) 2008; 101 Scope (10.1016/j.bpj.2010.08.017_bib11) 1973 Sinev (10.1016/j.bpj.2010.08.017_bib18) 1989; 180 Montgomery (10.1016/j.bpj.2010.08.017_bib37) 1977; 67 Tama (10.1016/j.bpj.2010.08.017_bib23) 2006; 35 Henzler-Wildman (10.1016/j.bpj.2010.08.017_bib6) 2007; 450 Ackerson (10.1016/j.bpj.2010.08.017_bib30) 1976; 64 Nägele (10.1016/j.bpj.2010.08.017_bib32) 1996; 272 Pickover (10.1016/j.bpj.2010.08.017_bib19) 1979; 254 Case (10.1016/j.bpj.2010.08.017_bib2) 1994; 4 Banks (10.1016/j.bpj.2010.08.017_bib13) 1979; 279 Henderson (10.1016/j.bpj.2010.08.017_bib20) 1994; 53 |
References_xml | – volume: 204 start-page: 327 year: 1996 end-page: 336 ident: bib17 article-title: Low frequency motions in phosphoglycerate kinase: a normal mode analysis publication-title: Chem. Phys. contributor: fullname: Mouawad – volume: 385 start-page: 275 year: 1997 end-page: 278 ident: bib16 article-title: Synergistic effects of substrate-induced changes in phosphoglycerate kinase activation publication-title: Nature contributor: fullname: Hol – volume: 13 start-page: 373 year: 2005 end-page: 380 ident: bib24 article-title: Usefulness and limitations of normal mode analysis in modeling dynamics of biomolecular complexes publication-title: Structure contributor: fullname: Ma – volume: 76 start-page: 1279 year: 1981 end-page: 1282 ident: bib31 article-title: Interpretation of the intermediate scattering function at short times publication-title: J. Chem. Phys. contributor: fullname: Tough – volume: 64 start-page: 242 year: 1976 end-page: 246 ident: bib30 article-title: Correlations for interacting Brownian particles publication-title: J. Chem. Phys. contributor: fullname: Ackerson – volume: 53 start-page: 95 year: 1994 end-page: 104 ident: bib20 article-title: Conformational changes in yeast phosphoglycerate kinase upon substrate binding publication-title: Biophys. Chem. contributor: fullname: Bunick – volume: 75 start-page: 4848 year: 1978 end-page: 4852 ident: bib5 article-title: Glucose-induced conformational change in yeast hexokinase publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Steitz – volume: 231 start-page: 840 year: 1993 end-page: 848 ident: bib21 article-title: Configurational distribution of denatured phosphoglycerate kinase publication-title: J. Mol. Biol. contributor: fullname: Smith – volume: 8 start-page: 1433 year: 1975 end-page: 1440 ident: bib29 article-title: The dynamics of interacting Brownian particles publication-title: J. Phys. A. contributor: fullname: Pusey – volume: 247 start-page: 14 year: 1974 end-page: 17 ident: bib12 article-title: Structure of yeast phosphoglycerate kinase publication-title: Nature contributor: fullname: Wendell – start-page: 335 year: 1973 end-page: 351 ident: bib11 publication-title: The Enzymes contributor: fullname: Scope – volume: 27 start-page: 213 year: 1982 end-page: 227 ident: bib33 article-title: A constrained regularization method for inverting data represented by linear algebraic or integral equations publication-title: Comput. Phys. Commun. contributor: fullname: Provencher – volume: 5 start-page: 513 year: 1998 end-page: 517 ident: bib3 article-title: Protein dynamics from NMR publication-title: Nat. Struct. Biol. contributor: fullname: Kay – start-page: 309 year: 2006 end-page: 547 ident: bib4 publication-title: Neutron Scattering in Biology – volume: 272 start-page: 215 year: 1996 end-page: 372 ident: bib32 article-title: On the dynamics and structure of charge-stabilized suspensions publication-title: Phys. Rep. contributor: fullname: Nägele – volume: 101 start-page: 118 year: 1956 end-page: 129 ident: bib41 article-title: Dynamics of neutron scattering molecules publication-title: Phys. Rev. contributor: fullname: Glauber – volume: 89 start-page: 11764 year: 1992 end-page: 11768 ident: bib22 article-title: Domain motions in phosphoglycerate kinase: Determination of interdomain distance distributions by site-specific labeling and time-resolved fluorescence energy transfer publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Mas – volume: 279 start-page: 773 year: 1979 end-page: 777 ident: bib13 article-title: Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme publication-title: Nature contributor: fullname: Phillips – volume: 32 start-page: W610 year: 2004 end-page: W614 ident: bib28 article-title: ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement publication-title: Nucleic Acids Res. contributor: fullname: Sanejouand – volume: 67 start-page: 4589 year: 1977 end-page: 4596 ident: bib37 article-title: The effects of hydrodynamic interactions on translational and rotational relaxation publication-title: J. Chem. Phys. contributor: fullname: Berne – volume: 5 start-page: 1475 year: 1997 end-page: 1483 ident: bib14 article-title: Closed structure of phosphoglycerate kinase from publication-title: Structure contributor: fullname: Jacob – volume: 77 start-page: 1905 year: 1996 end-page: 1908 ident: bib25 article-title: Large amplitude elastic motions in proteins from a single-parameter, atomic analysis publication-title: Phys. Rev. Lett. contributor: fullname: Tirion – volume: 12 start-page: 133 year: 1992 end-page: 144 ident: bib15 article-title: Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate publication-title: Proteins contributor: fullname: Blake – volume: 254 start-page: 11323 year: 1979 end-page: 11329 ident: bib19 article-title: Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase publication-title: J. Biol. Chem. contributor: fullname: Steitz – year: 1987 ident: bib1 article-title: Dynamics of Proteins and Nucleic Acids contributor: fullname: Harvey – volume: 102 start-page: 17646 year: 2005 end-page: 17651 ident: bib10 article-title: Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Callaway – volume: 123 year: 2005 ident: bib44 article-title: Reaction barrier heights from an exact-exchange-based density-functional correlation model publication-title: J. Chem. Phys. contributor: fullname: Becke – volume: 180 start-page: 61 year: 1989 end-page: 66 ident: bib18 article-title: Correlation between enzyme activity and hinge-bending domain displacement in 3-phosphoglycerate kinase publication-title: Eur. J. Biochem. contributor: fullname: Ptitsyn – volume: 450 start-page: 838 year: 2007 end-page: 844 ident: bib6 article-title: Intrinsic motions along an enzymatic reaction trajectory publication-title: Nature contributor: fullname: Kern – volume: 52 start-page: 2707 year: 1995 end-page: 2717 ident: bib36 article-title: Rotational diffusion in concentrated colloidal dispersions of hard spheres publication-title: Phys. Rev. E Stat. Phys. Plasmas Fluids Relat. Interdiscip. Topics contributor: fullname: Jones – volume: 399 start-page: 301 year: 1997 end-page: 323 ident: bib26 article-title: The Jülich neutron spin-echo spectrometer—Design and performance publication-title: Nucl. Instr. Meth. Phys. Res. A contributor: fullname: Richter – volume: 24 start-page: 1769 year: 1985 end-page: 1784 ident: bib9 article-title: Segmental flexibility in pig immunoglobulin G studied by neutron spin-echo technique publication-title: Biopolymers contributor: fullname: Ostanevich – volume: 42 start-page: 109 year: 1981 end-page: 118 ident: bib27 article-title: An analytic structure factor for macroion solutions publication-title: Mol. Phys. contributor: fullname: Penfold – volume: 78 start-page: 719 year: 2000 end-page: 730 ident: bib39 article-title: Calculation of hydrodynamic properties of globular proteins from their atomic-level structure publication-title: Biophys. J. contributor: fullname: Carrasco – volume: 101 start-page: 138102 year: 2008 ident: bib7 article-title: Direct observation of correlated interdomain motion in alcohol dehydrogenase publication-title: Phys. Rev. Lett. contributor: fullname: Richter – volume: 33 start-page: 6739 year: 1994 end-page: 6749 ident: bib8 article-title: Structural mechanisms for domain movements in proteins publication-title: Biochemistry contributor: fullname: Chothia – volume: 9 start-page: 215 year: 1979 end-page: 221 ident: bib34 article-title: Some measurements of the shape and hydrodynamic properties of yeast phosphoglycerate kinase (E.C.2.7.2.3) publication-title: Biophys. Chem. contributor: fullname: Spragg – volume: 4 start-page: 285 year: 1994 end-page: 290 ident: bib2 article-title: Normal-mode analysis of protein dynamics publication-title: Curr. Opin. Struct. Biol. contributor: fullname: Case – volume: 35 start-page: 115 year: 2006 end-page: 133 ident: bib23 article-title: Symmetry, form, and shape: guiding principles for robustness in macromolecular machines publication-title: Annu. Rev. Biophys. Biomol. Struct. contributor: fullname: Brooks – volume: 35 start-page: 4118 year: 1996 end-page: 4127 ident: bib42 article-title: Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate publication-title: Biochemistry contributor: fullname: Rees – volume: 128 start-page: 104903 year: 2008 ident: bib35 article-title: Short-time transport properties in dense suspensions: from neutral to charge-stabilized colloidal spheres publication-title: J. Chem. Phys. contributor: fullname: Nägele – volume: 259 start-page: 939 year: 1999 end-page: 945 ident: bib43 article-title: Site-directed mutagenesis of proline 204 in the ‘hinge’ region of yeast phosphoglycerate kinase publication-title: Eur. J. Biochem. contributor: fullname: Littlechild – volume: 38 start-page: 2614 year: 1988 end-page: 2626 ident: bib40 article-title: Effect of rotational diffusion on quasielastic light scattering from fractal colloid aggregates publication-title: Phys. Rev. A contributor: fullname: Meakin – volume: 14 start-page: 1 year: 1976 end-page: 10 ident: bib38 article-title: Quasielastic scattering by dilute polymer solutions publication-title: J. Polym. Sci., B Polym. Phys. Ed. contributor: fullname: Gurol – volume: 75 start-page: 4848 year: 1978 ident: 10.1016/j.bpj.2010.08.017_bib5 article-title: Glucose-induced conformational change in yeast hexokinase publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.75.10.4848 contributor: fullname: Bennett – volume: 399 start-page: 301 year: 1997 ident: 10.1016/j.bpj.2010.08.017_bib26 article-title: The Jülich neutron spin-echo spectrometer—Design and performance publication-title: Nucl. Instr. Meth. Phys. Res. A doi: 10.1016/S0168-9002(97)00956-X contributor: fullname: Monkenbusch – volume: 128 start-page: 104903 year: 2008 ident: 10.1016/j.bpj.2010.08.017_bib35 article-title: Short-time transport properties in dense suspensions: from neutral to charge-stabilized colloidal spheres publication-title: J. Chem. Phys. doi: 10.1063/1.2868773 contributor: fullname: Banchio – volume: 247 start-page: 14 year: 1974 ident: 10.1016/j.bpj.2010.08.017_bib12 article-title: Structure of yeast phosphoglycerate kinase publication-title: Nature doi: 10.1038/247014a0 contributor: fullname: Bryant – start-page: 309 year: 2006 ident: 10.1016/j.bpj.2010.08.017_bib4 – volume: 77 start-page: 1905 year: 1996 ident: 10.1016/j.bpj.2010.08.017_bib25 article-title: Large amplitude elastic motions in proteins from a single-parameter, atomic analysis publication-title: Phys. Rev. Lett. doi: 10.1103/PhysRevLett.77.1905 contributor: fullname: Tirion – volume: 35 start-page: 115 year: 2006 ident: 10.1016/j.bpj.2010.08.017_bib23 article-title: Symmetry, form, and shape: guiding principles for robustness in macromolecular machines publication-title: Annu. Rev. Biophys. Biomol. Struct. doi: 10.1146/annurev.biophys.35.040405.102010 contributor: fullname: Tama – volume: 67 start-page: 4589 year: 1977 ident: 10.1016/j.bpj.2010.08.017_bib37 article-title: The effects of hydrodynamic interactions on translational and rotational relaxation publication-title: J. Chem. Phys. doi: 10.1063/1.434619 contributor: fullname: Montgomery – volume: 78 start-page: 719 year: 2000 ident: 10.1016/j.bpj.2010.08.017_bib39 article-title: Calculation of hydrodynamic properties of globular proteins from their atomic-level structure publication-title: Biophys. J. doi: 10.1016/S0006-3495(00)76630-6 contributor: fullname: García De La Torre – volume: 32 start-page: W610 issue: Web Server issue year: 2004 ident: 10.1016/j.bpj.2010.08.017_bib28 article-title: ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkh368 contributor: fullname: Suhre – volume: 5 start-page: 1475 year: 1997 ident: 10.1016/j.bpj.2010.08.017_bib14 article-title: Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability publication-title: Structure doi: 10.1016/S0969-2126(97)00297-9 contributor: fullname: Auerbach – volume: 385 start-page: 275 year: 1997 ident: 10.1016/j.bpj.2010.08.017_bib16 article-title: Synergistic effects of substrate-induced changes in phosphoglycerate kinase activation publication-title: Nature doi: 10.1038/385275a0 contributor: fullname: Bernstein – volume: 35 start-page: 4118 year: 1996 ident: 10.1016/j.bpj.2010.08.017_bib42 article-title: Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate publication-title: Biochemistry doi: 10.1021/bi952500o contributor: fullname: McPhillips – year: 1987 ident: 10.1016/j.bpj.2010.08.017_bib1 contributor: fullname: McCammon – volume: 259 start-page: 939 year: 1999 ident: 10.1016/j.bpj.2010.08.017_bib43 article-title: Site-directed mutagenesis of proline 204 in the ‘hinge’ region of yeast phosphoglycerate kinase publication-title: Eur. J. Biochem. doi: 10.1046/j.1432-1327.1999.00133.x contributor: fullname: McHarg – volume: 279 start-page: 773 year: 1979 ident: 10.1016/j.bpj.2010.08.017_bib13 article-title: Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme publication-title: Nature doi: 10.1038/279773a0 contributor: fullname: Banks – volume: 254 start-page: 11323 year: 1979 ident: 10.1016/j.bpj.2010.08.017_bib19 article-title: Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)86488-8 contributor: fullname: Pickover – volume: 52 start-page: 2707 year: 1995 ident: 10.1016/j.bpj.2010.08.017_bib36 article-title: Rotational diffusion in concentrated colloidal dispersions of hard spheres publication-title: Phys. Rev. E Stat. Phys. Plasmas Fluids Relat. Interdiscip. Topics contributor: fullname: Degiorgio – volume: 64 start-page: 242 year: 1976 ident: 10.1016/j.bpj.2010.08.017_bib30 article-title: Correlations for interacting Brownian particles publication-title: J. Chem. Phys. doi: 10.1063/1.431957 contributor: fullname: Ackerson – volume: 123 year: 2005 ident: 10.1016/j.bpj.2010.08.017_bib44 article-title: Reaction barrier heights from an exact-exchange-based density-functional correlation model publication-title: J. Chem. Phys. contributor: fullname: Dickinson – volume: 24 start-page: 1769 year: 1985 ident: 10.1016/j.bpj.2010.08.017_bib9 article-title: Segmental flexibility in pig immunoglobulin G studied by neutron spin-echo technique publication-title: Biopolymers doi: 10.1002/bip.360240908 contributor: fullname: Alpert – volume: 101 start-page: 138102 year: 2008 ident: 10.1016/j.bpj.2010.08.017_bib7 article-title: Direct observation of correlated interdomain motion in alcohol dehydrogenase publication-title: Phys. Rev. Lett. doi: 10.1103/PhysRevLett.101.138102 contributor: fullname: Biehl – volume: 14 start-page: 1 year: 1976 ident: 10.1016/j.bpj.2010.08.017_bib38 article-title: Quasielastic scattering by dilute polymer solutions publication-title: J. Polym. Sci., B Polym. Phys. Ed. doi: 10.1002/pol.1976.180140101 contributor: fullname: Akcasu – volume: 12 start-page: 133 year: 1992 ident: 10.1016/j.bpj.2010.08.017_bib15 article-title: Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate publication-title: Proteins doi: 10.1002/prot.340120207 contributor: fullname: Harlos – volume: 101 start-page: 118 year: 1956 ident: 10.1016/j.bpj.2010.08.017_bib41 article-title: Dynamics of neutron scattering molecules publication-title: Phys. Rev. doi: 10.1103/PhysRev.101.118 contributor: fullname: Zemach – volume: 76 start-page: 1279 year: 1981 ident: 10.1016/j.bpj.2010.08.017_bib31 article-title: Interpretation of the intermediate scattering function at short times publication-title: J. Chem. Phys. doi: 10.1063/1.443146 contributor: fullname: Ackerson – volume: 53 start-page: 95 year: 1994 ident: 10.1016/j.bpj.2010.08.017_bib20 article-title: Conformational changes in yeast phosphoglycerate kinase upon substrate binding publication-title: Biophys. Chem. doi: 10.1016/0301-4622(94)00080-8 contributor: fullname: Henderson – volume: 5 start-page: 513 issue: Suppl year: 1998 ident: 10.1016/j.bpj.2010.08.017_bib3 article-title: Protein dynamics from NMR publication-title: Nat. Struct. Biol. doi: 10.1038/755 contributor: fullname: Kay – volume: 33 start-page: 6739 year: 1994 ident: 10.1016/j.bpj.2010.08.017_bib8 article-title: Structural mechanisms for domain movements in proteins publication-title: Biochemistry doi: 10.1021/bi00188a001 contributor: fullname: Gerstein – volume: 13 start-page: 373 year: 2005 ident: 10.1016/j.bpj.2010.08.017_bib24 article-title: Usefulness and limitations of normal mode analysis in modeling dynamics of biomolecular complexes publication-title: Structure doi: 10.1016/j.str.2005.02.002 contributor: fullname: Ma – volume: 4 start-page: 285 year: 1994 ident: 10.1016/j.bpj.2010.08.017_bib2 article-title: Normal-mode analysis of protein dynamics publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/S0959-440X(94)90321-2 contributor: fullname: Case – start-page: 335 year: 1973 ident: 10.1016/j.bpj.2010.08.017_bib11 contributor: fullname: Scope – volume: 231 start-page: 840 year: 1993 ident: 10.1016/j.bpj.2010.08.017_bib21 article-title: Configurational distribution of denatured phosphoglycerate kinase publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1993.1330 contributor: fullname: Calmettes – volume: 8 start-page: 1433 year: 1975 ident: 10.1016/j.bpj.2010.08.017_bib29 article-title: The dynamics of interacting Brownian particles publication-title: J. Phys. A. doi: 10.1088/0305-4470/8/9/012 contributor: fullname: Pusey – volume: 102 start-page: 17646 year: 2005 ident: 10.1016/j.bpj.2010.08.017_bib10 article-title: Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0503388102 contributor: fullname: Bu – volume: 89 start-page: 11764 year: 1992 ident: 10.1016/j.bpj.2010.08.017_bib22 article-title: Domain motions in phosphoglycerate kinase: Determination of interdomain distance distributions by site-specific labeling and time-resolved fluorescence energy transfer publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.89.24.11764 contributor: fullname: Haran – volume: 9 start-page: 215 year: 1979 ident: 10.1016/j.bpj.2010.08.017_bib34 article-title: Some measurements of the shape and hydrodynamic properties of yeast phosphoglycerate kinase (E.C.2.7.2.3) publication-title: Biophys. Chem. doi: 10.1016/0301-4622(79)85004-8 contributor: fullname: Smith – volume: 204 start-page: 327 year: 1996 ident: 10.1016/j.bpj.2010.08.017_bib17 article-title: Low frequency motions in phosphoglycerate kinase: a normal mode analysis publication-title: Chem. Phys. doi: 10.1016/0301-0104(95)00293-6 contributor: fullname: Guilbert – volume: 450 start-page: 838 year: 2007 ident: 10.1016/j.bpj.2010.08.017_bib6 article-title: Intrinsic motions along an enzymatic reaction trajectory publication-title: Nature doi: 10.1038/nature06410 contributor: fullname: Henzler-Wildman – volume: 272 start-page: 215 year: 1996 ident: 10.1016/j.bpj.2010.08.017_bib32 article-title: On the dynamics and structure of charge-stabilized suspensions publication-title: Phys. Rep. doi: 10.1016/0370-1573(95)00078-X contributor: fullname: Nägele – volume: 27 start-page: 213 year: 1982 ident: 10.1016/j.bpj.2010.08.017_bib33 article-title: A constrained regularization method for inverting data represented by linear algebraic or integral equations publication-title: Comput. Phys. Commun. doi: 10.1016/0010-4655(82)90173-4 contributor: fullname: Provencher – volume: 38 start-page: 2614 year: 1988 ident: 10.1016/j.bpj.2010.08.017_bib40 article-title: Effect of rotational diffusion on quasielastic light scattering from fractal colloid aggregates publication-title: Phys. Rev. A doi: 10.1103/PhysRevA.38.2614 contributor: fullname: Lindsay – volume: 180 start-page: 61 year: 1989 ident: 10.1016/j.bpj.2010.08.017_bib18 article-title: Correlation between enzyme activity and hinge-bending domain displacement in 3-phosphoglycerate kinase publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1989.tb14615.x contributor: fullname: Sinev – volume: 42 start-page: 109 year: 1981 ident: 10.1016/j.bpj.2010.08.017_bib27 article-title: An analytic structure factor for macroion solutions publication-title: Mol. Phys. doi: 10.1080/00268978100100091 contributor: fullname: Hayter |
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SubjectTerms | Biocatalysis Biophysics Construction Crystal structure Diffusion Displacement Dynamics Echo surveys Enzymes Fluctuation Kinases Kinetics Models, Molecular Neutron Diffraction Phosphoglycerate Kinase - chemistry Phosphoglycerate Kinase - metabolism Phosphorylation Protein Protein Structure, Secondary Protein Structure, Tertiary Proteins Saccharomyces cerevisiae - enzymology Scattering, Small Angle Spectroscopy Spectrum analysis Structure-Activity Relationship Time Factors |
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Title | Large Domain Fluctuations on 50-ns Timescale Enable Catalytic Activity in Phosphoglycerate Kinase |
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