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Volumn 52, Issue 32, 2013, Pages 5421-5429

Redefining the role of the quaternary shift in bacillus stearothermophilus phosphofructokinase

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC INHIBITION; BACILLUS STEAROTHERMOPHILUS; BINDING AFFINITIES; INHIBITORY COUPLING; PHOSPHOENOLPYRUVATES; PHOSPHOFRUCTOKINASE; PROTEIN DATA BANK; SUBSTRATE-BINDING;

EID: 84881641454     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4002503     Document Type: Article
Times cited : (8)

References (31)
  • 1
    • 0014413329 scopus 로고
    • Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli
    • Blangy, D., Buc, H., and Monod, J. (1968) Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli J. Mol. Biol. 31, 13-35
    • (1968) J. Mol. Biol. , vol.31 , pp. 13-35
    • Blangy, D.1    Buc, H.2    Monod, J.3
  • 2
    • 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
  • 3
    • 0025189804 scopus 로고
    • Structural basis of the allosteric behaviour of phosphofructokinase
    • Schirmer, T. and Evans, P. R. (1990) Structural basis of the allosteric behaviour of phosphofructokinase Nature 343, 140-145
    • (1990) Nature , vol.343 , pp. 140-145
    • Schirmer, T.1    Evans, P.R.2
  • 4
    • 0018353474 scopus 로고
    • Structure and control of phosphofructokinase from Bacillus stearothermophilus
    • Evans, P. R. and Hudson, P. J. (1979) Structure and control of phosphofructokinase from Bacillus stearothermophilus Nature 279, 500-504
    • (1979) Nature , vol.279 , pp. 500-504
    • Evans, P.R.1    Hudson, P.J.2
  • 8
    • 1542350030 scopus 로고    scopus 로고
    • Quantitative analysis and interpretation of allosteric behavior
    • Reinhart, G. D. (2004) Quantitative analysis and interpretation of allosteric behavior Methods Enzymol. 380, 187-203
    • (2004) Methods Enzymol. , vol.380 , pp. 187-203
    • Reinhart, G.D.1
  • 9
    • 0034635971 scopus 로고    scopus 로고
    • Reevaluation of the accepted allosteric mechanism of phosphofructokinase from Bacillus stearothermophilus
    • Kimmel, J. L. and Reinhart, G. D. (2000) Reevaluation of the accepted allosteric mechanism of phosphofructokinase from Bacillus stearothermophilus Proc. Natl. Acad. Sci. U.S.A. 97, 3844-3849
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3844-3849
    • Kimmel, J.L.1    Reinhart, G.D.2
  • 10
    • 0347724018 scopus 로고    scopus 로고
    • Disentangling the web of allosteric communication in a homotetramer: Heterotropic inhibition of phosphofructokinase from Bacillus stearothermophilus
    • Ortigosa, A. D., Kimmel, J. L., and Reinhart, G. D. (2004) Disentangling the web of allosteric communication in a homotetramer: Heterotropic inhibition of phosphofructokinase from Bacillus stearothermophilus Biochemistry 43, 577-586
    • (2004) Biochemistry , vol.43 , pp. 577-586
    • Ortigosa, A.D.1    Kimmel, J.L.2    Reinhart, G.D.3
  • 11
    • 0023496222 scopus 로고
    • High-level expression of Bacillus stearothermophilus 6-phosphofructo-1- kinase in Escherichia coli
    • French, B. A., Valdez, B. C., Younathan, E. S., and Chang, S. H. (1987) High-level expression of Bacillus stearothermophilus 6-phosphofructo-1-kinase in Escherichia coli Gene 59, 279-283
    • (1987) Gene , vol.59 , pp. 279-283
    • French, B.A.1    Valdez, B.C.2    Younathan, E.S.3    Chang, S.H.4
  • 12
    • 33645420000 scopus 로고    scopus 로고
    • Construction of an inducible, pfkA and pfkB deficient strain of Escherichia coli for the expression and purification of phosphofructokinase from bacterial sources
    • Lovingshimer, M. R., Siegele, D., and Reinhart, G. D. (2006) Construction of an inducible, pfkA and pfkB deficient strain of Escherichia coli for the expression and purification of phosphofructokinase from bacterial sources Protein Expression Purif. 46, 475-482
    • (2006) Protein Expression Purif. , vol.46 , pp. 475-482
    • Lovingshimer, M.R.1    Siegele, D.2    Reinhart, G.D.3
  • 13
    • 0024494131 scopus 로고
    • Site-directed mutagenesis in Bacillus stearothermophilus fructose-6-phosphate 1-kinase. Mutation at the substrate-binding site affects allosteric behavior
    • Valdez, B. C., French, B. A., Younathan, E. S., and Chang, S. H. (1989) Site-directed mutagenesis in Bacillus stearothermophilus fructose-6-phosphate 1-kinase. Mutation at the substrate-binding site affects allosteric behavior J. Biol. Chem. 264, 131-135
    • (1989) J. Biol. Chem. , vol.264 , pp. 131-135
    • Valdez, B.C.1    French, B.A.2    Younathan, E.S.3    Chang, S.H.4
  • 14
    • 0035814907 scopus 로고    scopus 로고
    • Equilibrium binding studies of a tryptophan-shifted mutant of phosphofructokinase from Bacillus stearothermophilus
    • Riley-Lovingshimer, M. R. and Reinhart, G. D. (2001) Equilibrium binding studies of a tryptophan-shifted mutant of phosphofructokinase from Bacillus stearothermophilus Biochemistry 40, 3002-3008
    • (2001) Biochemistry , vol.40 , pp. 3002-3008
    • Riley-Lovingshimer, M.R.1    Reinhart, G.D.2
  • 15
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., Minor, W., and Carter, C. W., Jr. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2    Carter, Jr.C.W.3
  • 16
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath, J. W. (1999) The finer things in X-ray diffraction data collection Acta Crystallogr. D55, 1718-1725
    • (1999) Acta Crystallogr. , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 17
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A. J. (2007) Solving structures of protein complexes by molecular replacement with Phaser Acta Crystallogr. D63, 32-41
    • (2007) Acta Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 19
  • 20
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N., and Murshudov, G. N. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallogr. D57, 122-133
    • (2001) Acta Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 21
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 23
    • 84944486386 scopus 로고
    • A new mathematical treatment of changes of ionic concentration in muscle and nerve under the action of electric currents, with a theory as to their mode of excitation
    • Hill, A. V. (1910) A new mathematical treatment of changes of ionic concentration in muscle and nerve under the action of electric currents, with a theory as to their mode of excitation J. Physiol. 40, 190-224
    • (1910) J. Physiol. , vol.40 , pp. 190-224
    • Hill, A.V.1
  • 24
    • 0020794102 scopus 로고
    • The determination of thermodynamic allosteric paramters of an enzyme undergoing steady-state turnover
    • Reinhart, G. D. (1983) The determination of thermodynamic allosteric paramters of an enzyme undergoing steady-state turnover Arch. Biochem. Biophys. 224, 389-401
    • (1983) Arch. Biochem. Biophys. , vol.224 , pp. 389-401
    • Reinhart, G.D.1
  • 25
    • 0024023247 scopus 로고
    • Linked-function origins of cooperativity in a symmetrical dimer
    • Reinhart, G. D. (1988) Linked-function origins of cooperativity in a symmetrical dimer Biophys. Chem. 30, 159-172
    • (1988) Biophys. Chem. , vol.30 , pp. 159-172
    • Reinhart, G.D.1
  • 26
    • 84856278773 scopus 로고    scopus 로고
    • Structure of the apo form of Bacillus stearothermophilus phosphofructokinase
    • Mosser, R., Reddy, M. C., Bruning, J. B., Sacchettini, J. C., and Reinhart, G. D. (2012) Structure of the apo form of Bacillus stearothermophilus phosphofructokinase Biochemistry 51, 769-775
    • (2012) Biochemistry , vol.51 , pp. 769-775
    • Mosser, R.1    Reddy, M.C.2    Bruning, J.B.3    Sacchettini, J.C.4    Reinhart, G.D.5
  • 28
    • 0028272224 scopus 로고
    • Comparison of the inhibition by phospho(enol)pyruvate and phosphoglycolate of phosphofructokinase from B stearothermophilus
    • Tlapak-Simmons, V. L. and Reinhart, G. D. (1994) Comparison of the inhibition by phospho(enol)pyruvate and phosphoglycolate of phosphofructokinase from B. stearothermophilus Arch. Biochem. Biophys. 308, 226-230
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 226-230
    • Tlapak-Simmons, V.L.1    Reinhart, G.D.2
  • 30
    • 32344434479 scopus 로고    scopus 로고
    • The changing landscape of protein allostery
    • Swain, J. F. and Gierasch, L. M. (2006) The changing landscape of protein allostery Curr. Opin. Struct. Biol. 16, 102-108
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 102-108
    • Swain, J.F.1    Gierasch, L.M.2
  • 31
    • 0016697729 scopus 로고
    • Cooperativity of binding of anilinonaphthalenesulfonate to serum albumin induced by a second ligand
    • Kolb, D. A. and Weber, G. (1975) Cooperativity of binding of anilinonaphthalenesulfonate to serum albumin induced by a second ligand Biochemistry 14, 4476-4481
    • (1975) Biochemistry , vol.14 , pp. 4476
    • Kolb, D.A.1    Weber, G.2


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