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Volumn 291, Issue 17, 2016, Pages 9244-9256

Conformational dynamics and allostery in pyruvate kinase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BINS; DEUTERIUM; DIGITAL STORAGE; DYNAMICS; ELECTROSPRAY IONIZATION; ENZYMES; ESCHERICHIA COLI; FRUCTOSE; MASS SPECTROMETRY; MONOMERS; OLIGOMERS; RIGID STRUCTURES; ROTATION;

EID: 84965005994     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.676270     Document Type: Article
Times cited : (29)

References (53)
  • 1
    • 50449109973 scopus 로고    scopus 로고
    • Allostery: An illustrated definition for the second secret of life
    • Fenton, A. W. (2008) Allostery: an illustrated definition for the second secret of life. Trends Biochem. Sci. 33, 420-425
    • (2008) Trends Biochem. Sci , vol.33 , pp. 420-425
    • Fenton, A.W.1
  • 2
    • 84888333782 scopus 로고    scopus 로고
    • 50 years of allosteric interactions: The twists and turns of the models
    • Changeux, J. P. (2013) 50 years of allosteric interactions: the twists and turns of the models. Nat. Rev. Mol. Cell Biol. 14, 819-829
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 819-829
    • Changeux, J.P.1
  • 3
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • Monod, J., and Changeux., J. P., and Jacob, F. (1963) Allosteric proteins and cellular control systems. J. Mol. Biol. 6, 306-329
    • (1963) J. Mol. Biol , vol.6 , pp. 306-329
    • Monod, J.1    Changeux, J.P.2    Jacob, F.3
  • 4
    • 84923673779 scopus 로고    scopus 로고
    • New look at hemoglobin allostery
    • Yuan, Y., and Tam., M. F., Simplaceanu, V., and Ho, C. (2015) New look at hemoglobin allostery. Chem. Rev. 115, 1702-1724
    • (2015) Chem. Rev , vol.115 , pp. 1702-1724
    • Yuan, Y.1    Tam, M.F.2    Simplaceanu, V.3    Ho, C.4
  • 5
    • 68149157248 scopus 로고    scopus 로고
    • The origin of allosteric functional modulation: Multiple pre-existing pathways
    • del Sol, A., Tsai, C. J., Ma, B., and Nussinov, R. (2009) The origin of allosteric functional modulation: multiple pre-existing pathways. Structure 17, 1042-1050
    • (2009) Structure , vol.17 , pp. 1042-1050
    • Del Sol, A.1    Tsai, C.J.2    Ma, B.3    Nussinov, R.4
  • 6
    • 0029610838 scopus 로고
    • Cloning of the two pyruvate kinase isoenzyme structural genes from Escherichia coli: The relative roles of these enzymes in pyruvate biosynthesis
    • Ponce, E., Flores, N., Martinez, A., Valle, F., and Bolívar, F. (1995) Cloning of the two pyruvate kinase isoenzyme structural genes from Escherichia coli: the relative roles of these enzymes in pyruvate biosynthesis. J. Bacteriol. 177, 5719-5722
    • (1995) J. Bacteriol , vol.177 , pp. 5719-5722
    • Ponce, E.1    Flores, N.2    Martinez, A.3    Valle, F.4    Bolívar, F.5
  • 8
    • 0029645125 scopus 로고
    • Crystal structure of Escherichia coli pyruvate kinase type I: Molecular basis of the allosteric transition
    • Mattevi, A., Valentini, G., Rizzi, M., Speranza, M. L., Bolognesi, M., and Coda, A. (1995) Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition. Structure 3, 729-741
    • (1995) Structure , vol.3 , pp. 729-741
    • Mattevi, A.1    Valentini, G.2    Rizzi, M.3    Speranza, M.L.4    Bolognesi, M.5    Coda, A.6
  • 9
    • 84896316278 scopus 로고    scopus 로고
    • Regulation of pyruvate metabolism in metabolic-related diseases
    • Jeoung, N.H., Harris, C. R., and Harris, R.A. (2014) Regulation of pyruvate metabolism in metabolic-related diseases. Rev. Endocr. Metab. Disord. 15, 99-110
    • (2014) Rev. Endocr. Metab. Disord , vol.15 , pp. 99-110
    • Jeoung, N.H.1    Harris, C.R.2    Harris, R.A.3
  • 11
    • 0032520197 scopus 로고    scopus 로고
    • The allosteric regulation of pyruvate kinase by fructose-1, 6-bisphosphate
    • Jurica, M. S., Mesecar, A., Heath, P. J., Shi, W., Nowak, T., and Stoddard, B. L. (1998) The allosteric regulation of pyruvate kinase by fructose-1, 6-bisphosphate. Structure 6, 195-210
    • (1998) Structure , vol.6 , pp. 195-210
    • Jurica, M.S.1    Mesecar, A.2    Heath, P.J.3    Shi, W.4    Nowak, T.5    Stoddard, B.L.6
  • 12
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J., and Changeux, J. P. (1965) On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88-118
    • (1965) J. Mol. Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 13
    • 0038241711 scopus 로고    scopus 로고
    • Pyruvate kinase: Current status of regulatory and functional properties
    • Munõoz, M. E., and Ponce, E. (2003) Pyruvate kinase: current status of regulatory and functional properties. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 135, 197-218
    • (2003) Comp. Biochem. Physiol. B Biochem. Mol. Biol , vol.135 , pp. 197-218
    • Munõoz, M.E.1    Ponce, E.2
  • 14
    • 0016610086 scopus 로고
    • The control of pyruvate kinases of Escherichia coli. II. Effectors and regulatory properties of the enzyme activated by ribose 5-phosphate
    • Waygood, E. B., and Rayman., M. K., and Sanwal, B. (1975) The control of pyruvate kinases of Escherichia coli. II. Effectors and regulatory properties of the enzyme activated by ribose 5-phosphate. Can. J. Biochem. 53, 444-454
    • (1975) Can. J. Biochem , vol.53 , pp. 444-454
    • Waygood, E.B.1    Rayman, M.K.2    Sanwal, B.3
  • 16
    • 0001381881 scopus 로고    scopus 로고
    • Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 Å
    • Allen, S. C., and Muirhead, H. (1996) Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 Å. Acta Crystallogr. D Biol. Crystallogr. 52, 499-504
    • (1996) Acta Crystallogr. D Biol. Crystallogr , vol.52 , pp. 499-504
    • Allen, S.C.1    Muirhead, H.2
  • 18
    • 0017813889 scopus 로고
    • Structure of pyruvate kinase and similarities with other enzymes: Possible implications for protein taxonomy and evolution
    • Levine, M., Muirhead, H., Stammers, D. K., and Stuart, D. I. (1978) Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution. Nature 271, 626-630
    • (1978) Nature , vol.271 , pp. 626-630
    • Levine, M.1    Muirhead, H.2    Stammers, D.K.3    Stuart, D.I.4
  • 19
    • 79958162511 scopus 로고    scopus 로고
    • Effects of ions on ligand binding to pyruvate kinase: Mapping the binding site with infrared spectroscopy
    • Kumar, S., and Barth, A. (2011) Effects of ions on ligand binding to pyruvate kinase: mapping the binding site with infrared spectroscopy. J. Phys. Chem. B 115, 6784-6789
    • (2011) J. Phys. Chem. B , vol.115 , pp. 6784-6789
    • Kumar, S.1    Barth, A.2
  • 20
    • 84923372043 scopus 로고    scopus 로고
    • Distinguishing the interactions in the fructose-1, 6-bisphosphate binding site of human liver pyruvate kinase that contribute to allostery
    • Ishwar, A., Tang, Q., and Fenton, A. W. (2015) Distinguishing the interactions in the fructose-1, 6-bisphosphate binding site of human liver pyruvate kinase that contribute to allostery. Biochemistry 54, 1516-1524
    • (2015) Biochemistry , vol.54 , pp. 1516-1524
    • Ishwar, A.1    Tang, Q.2    Fenton, A.W.3
  • 22
    • 0030600132 scopus 로고    scopus 로고
    • The allosteric regulation of pyruvate kinase
    • Mattevi, A., Bolognesi, M., and Valentini, G. (1996) The allosteric regulation of pyruvate kinase. FEBS Lett. 389, 15-19
    • (1996) FEBS Lett , vol.389 , pp. 15-19
    • Mattevi, A.1    Bolognesi, M.2    Valentini, G.3
  • 23
    • 0030444081 scopus 로고    scopus 로고
    • New structures of allosteric proteins revealing remarkable conformational changes
    • Mattevi, A., Rizzi, M., and Bolognesi, M. (1996) New structures of allosteric proteins revealing remarkable conformational changes. Curr. Opin. Struct. Biol. 6, 824-829
    • (1996) Curr. Opin. Struct. Biol , vol.6 , pp. 824-829
    • Mattevi, A.1    Rizzi, M.2    Bolognesi, M.3
  • 24
    • 84895745240 scopus 로고    scopus 로고
    • Aunified view of "how allostery works."
    • Tsai, C. J., and Nussinov, R. (2014) Aunified view of "how allostery works." PLoS Comput. Biol. 10, e1003394
    • (2014) PLoS Comput. Biol , vol.10
    • Tsai, C.J.1    Nussinov, R.2
  • 25
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr, D. D., Nussinov, R., and Wright, P. E. (2009) The role of dynamic conformational ensembles in biomolecular recognition. Nat. Chem. Biol. 5, 789-796
    • (2009) Nat. Chem. Biol , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 26
    • 84898993517 scopus 로고    scopus 로고
    • The ensemble nature of allostery
    • Motlagh, H. N., and Wrabl., J. O., Li, J., and Hilser, V. J. (2014) The ensemble nature of allostery. Nature 508, 331-339
    • (2014) Nature , vol.508 , pp. 331-339
    • Motlagh, H.N.1    Wrabl, J.O.2    Li, J.3    Hilser, V.J.4
  • 27
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • Goodey, N. M., and Benkovic, S. J. (2008) Allosteric regulation and catalysis emerge via a common route. Nat. Chem. Biol. 4, 474-482
    • (2008) Nat. Chem. Biol , vol.4 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 28
    • 84891841002 scopus 로고    scopus 로고
    • Structural basis of the autophagyrelated LC3/Atg13 LIR complex: Recognition and interaction mechanism
    • Suzuki, H., Tabata, K., Morita, E., Kawasaki, M., Kato, R., Dobson, R. C., Yoshimori, T., and Wakatsuki, S. (2014) Structural basis of the autophagyrelated LC3/Atg13 LIR complex: recognition and interaction mechanism. Structure 22, 47-58
    • (2014) Structure , vol.22 , pp. 47-58
    • Suzuki, H.1    Tabata, K.2    Morita, E.3    Kawasaki, M.4    Kato, R.5    Dobson, R.C.6    Yoshimori, T.7    Wakatsuki, S.8
  • 29
    • 0020440318 scopus 로고
    • AMP- and fructose 1, 6-bisphosphate-activated pyruvate kinases from Escherichia coli
    • Malcovati, M., and Valentini, G. (1982) AMP- and fructose 1, 6-bisphosphate-activated pyruvate kinases from Escherichia coli. Methods Enzymol. 90, 170-179
    • (1982) Methods Enzymol , vol.90 , pp. 170-179
    • Malcovati, M.1    Valentini, G.2
  • 30
  • 31
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves
    • Hill, A. (1910) The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves. J. Phys. 40, i-vii
    • (1910) J. Phys , vol.40 , pp. i-vii
    • Hill, A.1
  • 32
    • 84859904015 scopus 로고    scopus 로고
    • Measuring dynamics in weakly structured regions of proteins using microfluidics-enabled subsecond H/D exchange mass spectrometry
    • Rob, T., Liuni, P., Gill, P. K., Zhu, S., Balachandran, N., Berti, P. J., and Wilson, D. J. (2012) Measuring dynamics in weakly structured regions of proteins using microfluidics-enabled subsecond H/D exchange mass spectrometry. Anal. Chem. 84, 3771-3779
    • (2012) Anal. Chem , vol.84 , pp. 3771-3779
    • Rob, T.1    Liuni, P.2    Gill, P.K.3    Zhu, S.4    Balachandran, N.5    Berti, P.J.6    Wilson, D.J.7
  • 33
    • 57649220030 scopus 로고    scopus 로고
    • A versatile microfluidic chip for millisecond time-scale kinetic studies by electrospray mass spectrometry
    • Rob, T., and Wilson, D. J. (2009) A versatile microfluidic chip for millisecond time-scale kinetic studies by electrospray mass spectrometry. J. Am. Soc. Mass Spectrom. 20, 124-130
    • (2009) J. Am. Soc. Mass Spectrom , vol.20 , pp. 124-130
    • Rob, T.1    Wilson, D.J.2
  • 34
    • 0345600790 scopus 로고    scopus 로고
    • A capillary mixer with adjustable reaction chamber volume for millisecond time-resolved studies by electrospray mass spectrometry
    • Wilson, D.J., and Konermann, L. (2003) A capillary mixer with adjustable reaction chamber volume for millisecond time-resolved studies by electrospray mass spectrometry. Anal. Chem. 75, 6408-6414
    • (2003) Anal. Chem , vol.75 , pp. 6408-6414
    • Wilson, D.J.1    Konermann, L.2
  • 35
    • 72049118729 scopus 로고    scopus 로고
    • The quaternary structure of pyruvate kinase type 1 from Escherichia coli at low nanomolar concentrations
    • Zhu, T., and Bailey., M. F., Angley, L. M., Cooper, T. F., and Dobson, R. C. (2010) The quaternary structure of pyruvate kinase type 1 from Escherichia coli at low nanomolar concentrations. Biochimie 92, 116-120
    • (2010) Biochimie , vol.92 , pp. 116-120
    • Zhu, T.1    Bailey, M.F.2    Angley, L.M.3    Cooper, T.F.4    Dobson, R.C.5
  • 36
    • 0036323612 scopus 로고    scopus 로고
    • Kinetic and allosteric consequences of mutations in the subunit and domain interfaces and the allosteric site of yeast pyruvate kinase
    • Fenton, A. W., and Blair, J. B. (2002) Kinetic and allosteric consequences of mutations in the subunit and domain interfaces and the allosteric site of yeast pyruvate kinase. Arch. Biochem. Biophys. 397, 28-39
    • (2002) Arch. Biochem. Biophys , vol.397 , pp. 28-39
    • Fenton, A.W.1    Blair, J.B.2
  • 37
    • 0020771563 scopus 로고
    • Analysis of progress curves. Interaction of pyruvate kinase from Escherichia coli with fructose 1, 6-bisphosphate and calciumions
    • Boiteux, A., Markus, M., Plesser, T., Hess, B., and Malcovati, M. (1983) Analysis of progress curves. Interaction of pyruvate kinase from Escherichia coli with fructose 1, 6-bisphosphate and calciumions. Biochem. J. 211, 631-640
    • (1983) Biochem. J , vol.211 , pp. 631-640
    • Boiteux, A.1    Markus, M.2    Plesser, T.3    Hess, B.4    Malcovati, M.5
  • 38
    • 84911370403 scopus 로고    scopus 로고
    • Changes in signal transducer and activator of transcription 3 (STAT3) dynamics induced by complexation with pharmacological inhibitors of src homology 2 (SH2) domain dimerization
    • Resetca, D., Haftchenary, S., Gunning, P. T., and Wilson, D. J. (2014) Changes in signal transducer and activator of transcription 3 (STAT3) dynamics induced by complexation with pharmacological inhibitors of Src homology 2 (SH2) domain dimerization. J. Biol. Chem. 289, 32538-32547
    • (2014) J. Biol. Chem , vol.289 , pp. 32538-32547
    • Resetca, D.1    Haftchenary, S.2    Gunning, P.T.3    Wilson, D.J.4
  • 39
    • 77952980825 scopus 로고    scopus 로고
    • Mmass 3: A cross-platform software environment for precise analysis of mass spectrometric data
    • Strohalm, M., Kavan, D., Novák, P., Volny, M., and Havlícek, V. (2010) mMass 3: a cross-platform software environment for precise analysis of mass spectrometric data. Anal. Chem. 82, 4648-4651
    • (2010) Anal. Chem , vol.82 , pp. 4648-4651
    • Strohalm, M.1    Kavan, D.2    Novák, P.3    Volny, M.4    Havlícek, V.5
  • 41
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., and Sligar., S. G., and Wolynes, P. G. (1991) The energy landscapes and motions of proteins. Science 254, 1598-1603
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 42
    • 79960189344 scopus 로고    scopus 로고
    • Dynamic allostery: Linkers are not merely flexible
    • Ma, B., and Tsai., C. J., Haliloglu, T., and Nussinov, R. (2011) Dynamic allostery: linkers are not merely flexible. Structure 19, 907-917
    • (2011) Structure , vol.19 , pp. 907-917
    • Ma, B.1    Tsai, C.J.2    Haliloglu, T.3    Nussinov, R.4
  • 43
    • 84916887461 scopus 로고    scopus 로고
    • Allostery without a conformational change? Revisiting the paradigm
    • Nussinov, R., and Tsai, C J. (2015) Allostery without a conformational change? Revisiting the paradigm. Curr. Opin. Struct. Biol. 30, 17-24
    • (2015) Curr. Opin. Struct. Biol , vol.30 , pp. 17-24
    • Nussinov, R.1    Tsai, C.J.2
  • 44
    • 64849111005 scopus 로고    scopus 로고
    • Sending signals dynamically
    • Smock, R. G., and Gierasch, L. M. (2009) Sending signals dynamically. Science 324, 198-203
    • (2009) Science , vol.324 , pp. 198-203
    • Smock, R.G.1    Gierasch, L.M.2
  • 45
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • Boehr, D. D., McElheny, D., Dyson, H. J., and Wright, P. E. (2006) The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313, 1638-1642
    • (2006) Science , vol.313 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wright, P.E.4
  • 46
    • 84866392040 scopus 로고    scopus 로고
    • Conformer selection and intensified dynamics during catalytic turnover in chymotrypsin
    • Liuni, P., Jeganathan, A., and Wilson, D. J. (2012) Conformer selection and intensified dynamics during catalytic turnover in chymotrypsin. Angew. Chem. Int. Ed. Engl. 51, 9666-9669
    • (2012) Angew. Chem. Int. Ed. Engl , vol.51 , pp. 9666-9669
    • Liuni, P.1    Jeganathan, A.2    Wilson, D.J.3
  • 47
    • 80052397343 scopus 로고    scopus 로고
    • The trypanocidal drug suramin and other trypan blue mimetics are inhibitors of pyruvate kinases and bind to the adenosine site
    • Morgan, H. P., and McNae., I. W., Nowicki, M. W., Zhong, W., Michels, P. A., Auld, D.S., Fothergill-Gilmore, L. A., and Walkinshaw, M. D. (2011) The trypanocidal drug suramin and other trypan blue mimetics are inhibitors of pyruvate kinases and bind to the adenosine site. J. Biol. Chem. 286, 31232-31240
    • (2011) J. Biol. Chem , vol.286 , pp. 31232-31240
    • Morgan, H.P.1    McNae, I.W.2    Nowicki, M.W.3    Zhong, W.4    Michels, P.A.5    Auld, D.S.6    Fothergill-Gilmore, L.A.7    Walkinshaw, M.D.8
  • 48
    • 0026490822 scopus 로고
    • Key residues in the allosteric transition of bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis
    • Walker, D., Chia, W. N, and Muirhead, H. (1992) Key residues in the allosteric transition of Bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis. J. Mol. Biol. 228, 265-276
    • (1992) J. Mol. Biol , vol.228 , pp. 265-276
    • Walker, D.1    Chia, W.N.2    Muirhead, H.3
  • 49
    • 0032489428 scopus 로고    scopus 로고
    • Cooperativity in bacillus stearothermophilus pyruvate kinase
    • Lovell, S. C, Mullick, A. H., and Muirhead, H. (1998) Cooperativity in Bacillus stearothermophilus pyruvate kinase. J. Mol. Biol. 276, 839-851
    • (1998) J. Mol. Biol , vol.276 , pp. 839-851
    • Lovell, S.C.1    Mullick, A.H.2    Muirhead, H.3
  • 50
    • 0027087368 scopus 로고
    • The importance of surface loops for stabilizing an eightfold βα Barrel protein
    • Urfer, R., and Kirschner, K. (1992) The importance of surface loops for stabilizing an eightfold βα barrel protein. Protein Sci. 1, 31-45
    • (1992) Protein Sci , vol.1 , pp. 31-45
    • Urfer, R.1    Kirschner, K.2
  • 52
    • 77955674424 scopus 로고    scopus 로고
    • Changes in small angle x-ray scattering parameters observed upon ligand binding to rabbit muscle pyruvate kinase are not correlated with allosteric transitions
    • Fenton, A. W., Williams, R., and Trewhella, J. (2010) Changes in small angle x-ray scattering parameters observed upon ligand binding to rabbit muscle pyruvate kinase are not correlated with allosteric transitions. Biochemistry 49, 7202-7209
    • (2010) Biochemistry , vol.49 , pp. 7202-7209
    • Fenton, A.W.1    Williams, R.2    Trewhella, J.3


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