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Volumn 326, Issue 5, 2003, Pages 1513-1522

P but not R-axis interface is involved in cooperative binding of NAD on tetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus

Author keywords

Cooperativity; D glyceraldehyde 3 phosphate dehydrogenase; Dimers; NAD; Small angle X ray scattering

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 0037424625     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00049-4     Document Type: Article
Times cited : (20)

References (27)
  • 1
    • 0023644310 scopus 로고
    • Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution
    • Skarzynski T., Moody P.C., Wonacott A.J. Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution. J. Mol. Biol. 193:1987;171-187.
    • (1987) J. Mol. Biol. , vol.193 , pp. 171-187
    • Skarzynski, T.1    Moody, P.C.2    Wonacott, A.J.3
  • 2
    • 0023717499 scopus 로고
    • Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
    • Skarzynski T., Wonacott A.J. Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. J. Mol. Biol. 203:1988;1097-1118.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1097-1118
    • Skarzynski, T.1    Wonacott, A.J.2
  • 3
    • 0033534147 scopus 로고    scopus 로고
    • Dimers generated from tetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus are inactive but exhibit cooperativity in NAD binding
    • Roitel O., Sergienko E., Branlant G. Dimers generated from tetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus are inactive but exhibit cooperativity in NAD binding. Biochemistry. 38:1999;16084-16091.
    • (1999) Biochemistry , vol.38 , pp. 16084-16091
    • Roitel, O.1    Sergienko, E.2    Branlant, G.3
  • 4
    • 0037129983 scopus 로고    scopus 로고
    • Thermal unfolding used as a probe to characterize the intra- and intersubunit stabilizing interactions in phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
    • Roitel O., Ivinova O., Muronetz V., Nagradova N., Branlant G. Thermal unfolding used as a probe to characterize the intra- and intersubunit stabilizing interactions in phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Biochemistry. 41:2002;7556-7564.
    • (2002) Biochemistry , vol.41 , pp. 7556-7564
    • Roitel, O.1    Ivinova, O.2    Muronetz, V.3    Nagradova, N.4    Branlant, G.5
  • 5
    • 0038058016 scopus 로고    scopus 로고
    • Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: Implication for NAD binding and cooperativity
    • Duee E., Olivier-Deyris L., Fanchon E., Corbier C., Branlant G., Dideberg O. Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity. J. Mol. Biol. 257:1996;814-838.
    • (1996) J. Mol. Biol. , vol.257 , pp. 814-838
    • Duee, E.1    Olivier-Deyris, L.2    Fanchon, E.3    Corbier, C.4    Branlant, G.5    Dideberg, O.6
  • 6
    • 84944815124 scopus 로고
    • Small-angle-scattering-data treatment by the regularization method
    • Svergun D., Semenyuk, Feigin L.A. Small-angle-scattering-data treatment by the regularization method. Acta Crystallog. sect., A. 44:1988;244-250.
    • (1988) Acta Crystallog. sect., A , vol.44 , pp. 244-250
    • Svergun, D.1    Semenyuk2    Feigin, L.A.3
  • 7
    • 0020407335 scopus 로고
    • Affinity labeling of glyceraldehyde-3-phosphate dehydrogenase from sturgeon and Bacillus stearothermophilus by 3-chloroacetylpyridine-adenine dinucleotide. Kinetic Studies
    • Branlant G., Eiler B., Wallen L., Biellmann J.F. Affinity labeling of glyceraldehyde-3-phosphate dehydrogenase from sturgeon and Bacillus stearothermophilus by 3-chloroacetylpyridine-adenine dinucleotide. Kinetic Studies. Eur. J. Biochem. 127:1982;519-524.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 519-524
    • Branlant, G.1    Eiler, B.2    Wallen, L.3    Biellmann, J.F.4
  • 8
    • 0032521628 scopus 로고    scopus 로고
    • Comparative study of the catalytic domain of phosphorylating glyceraldehyde-3-phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site-directed mutagenesis
    • Talfournier F., Colloc'h N., Mornon J.P., Branlant G. Comparative study of the catalytic domain of phosphorylating glyceraldehyde-3-phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site-directed mutagenesis. Eur. J. Biochem. 252:1998;447-457.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 447-457
    • Talfournier, F.1    Colloc'h, N.2    Mornon, J.P.3    Branlant, G.4
  • 9
    • 0024555940 scopus 로고
    • Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis
    • Soukri A., Mougin A., Corbier C., Wonacott A., Branlant C., Branlant G. Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis. Biochemistry. 28:1989;2586-2592.
    • (1989) Biochemistry , vol.28 , pp. 2586-2592
    • Soukri, A.1    Mougin, A.2    Corbier, C.3    Wonacott, A.4    Branlant, C.5    Branlant, G.6
  • 10
    • 0025197777 scopus 로고
    • The nicotinamide subsite of glyceraldehyde-3-phosphate dehydrogenase studied by site-directed mutagenesis
    • Corbier C., Mougin A., Mely Y., Adolph H.W., Zeppezauer M., Gerard D., et al. The nicotinamide subsite of glyceraldehyde-3-phosphate dehydrogenase studied by site-directed mutagenesis. Biochimie. 72:1990;545-554.
    • (1990) Biochimie , vol.72 , pp. 545-554
    • Corbier, C.1    Mougin, A.2    Mely, Y.3    Adolph, H.W.4    Zeppezauer, M.5    Gerard, D.6
  • 11
    • 0027383390 scopus 로고
    • Determinants of coenzyme specificity in glyceraldehyde-3-phosphate dehydrogenase: Role of the acidic residue in the fingerprint region of the nucleotide binding fold
    • Clermont S., Corbier C., Mely Y., Gerard D., Wonacott A., Branlant G. Determinants of coenzyme specificity in glyceraldehyde-3-phosphate dehydrogenase: role of the acidic residue in the fingerprint region of the nucleotide binding fold. Biochemistry. 32:1993;10178-10184.
    • (1993) Biochemistry , vol.32 , pp. 10178-10184
    • Clermont, S.1    Corbier, C.2    Mely, Y.3    Gerard, D.4    Wonacott, A.5    Branlant, G.6
  • 12
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland D.E. Jr, Nemethy G., Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry. 5:1966;365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland D.E., Jr.1    Nemethy, G.2    Filmer, D.3
  • 13
    • 0001195192 scopus 로고
    • The binding of nicotinamide-adenine dinucleotide to D-glyceraldehyde-3-phosphate dehydrogenase: Temperature jump relaxation studies on the mechanism of an allosteric enzyme
    • Kirschner K., Eigen M., Bittman R., Voigt B. The binding of nicotinamide-adenine dinucleotide to D-glyceraldehyde-3-phosphate dehydrogenase: temperature jump relaxation studies on the mechanism of an allosteric enzyme. Proc. Natl. Acad. Sci. USA. 56:1966;1661-1667.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.56 , pp. 1661-1667
    • Kirschner, K.1    Eigen, M.2    Bittman, R.3    Voigt, B.4
  • 14
    • 0014954234 scopus 로고
    • Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase
    • Cook R.A., Koshland D.E. Jr. Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase. Biochemistry. 9:1970;3337-3342.
    • (1970) Biochemistry , vol.9 , pp. 3337-3342
    • Cook, R.A.1    Koshland D.E., Jr.2
  • 15
    • 0015243230 scopus 로고
    • Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. II. Stopped-flow studies at pH 8-5 and 40 degrees C
    • Kirschner K. Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. II. Stopped-flow studies at pH 8-5 and 40 degrees C. J. Mol. Biol. 58:1971;51-68.
    • (1971) J. Mol. Biol. , vol.58 , pp. 51-68
    • Kirschner, K.1
  • 16
    • 0016776237 scopus 로고
    • The binding of nicotinamide-adenine dimucleotide to glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus
    • Allen G., Harris J.I. The binding of nicotinamide-adenine dimucleotide to glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus. Biochem. J. 151:1975;747-749.
    • (1975) Biochem. J. , vol.151 , pp. 747-749
    • Allen, G.1    Harris, J.I.2
  • 17
    • 0017132753 scopus 로고
    • Negative homotropic cooperativity and affinity heterogeneity: Preparation of yeast glyceraldehyde-3-phosphate dehydrogenase with maximal affinity homogeneity
    • Gennis L.S. Negative homotropic cooperativity and affinity heterogeneity: preparation of yeast glyceraldehyde-3-phosphate dehydrogenase with maximal affinity homogeneity. Proc. Natl Acad. Sci. USA. 73:1976;3928-3932.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 3928-3932
    • Gennis, L.S.1
  • 18
    • 0020513891 scopus 로고
    • Coenzyme binding in crystals of glyceraldehyde-3-phosphate dehydrogenase
    • Leslie A.G., Wonacott A.J. Coenzyme binding in crystals of glyceraldehyde-3-phosphate dehydrogenase. J. Mol. Biol. 165:1983;375-391.
    • (1983) J. Mol. Biol. , vol.165 , pp. 375-391
    • Leslie, A.G.1    Wonacott, A.J.2
  • 19
    • 0035311517 scopus 로고    scopus 로고
    • Mass spectrometry as a novel approach to probe cooperativity in multimeric enzymatic systems
    • Rogniaux H., Sanglier S., Strupat K., Azza S., Roitel O., Ball V., et al. Mass spectrometry as a novel approach to probe cooperativity in multimeric enzymatic systems. Anal. Biochem. 291:2001;48-61.
    • (2001) Anal. Biochem. , vol.291 , pp. 48-61
    • Rogniaux, H.1    Sanglier, S.2    Strupat, K.3    Azza, S.4    Roitel, O.5    Ball, V.6
  • 21
    • 0029095399 scopus 로고
    • X-ray scattering titration of the quaternary structure transition of aspartate transcarbamylase with a bisubstrate analogue: Influence of nucleotide effectors
    • Fetler L., Tauc P., Herve G., Moody M.F., Vachette P. X-ray scattering titration of the quaternary structure transition of aspartate transcarbamylase with a bisubstrate analogue: influence of nucleotide effectors. J. Mol. Biol. 251:1995;243-255.
    • (1995) J. Mol. Biol. , vol.251 , pp. 243-255
    • Fetler, L.1    Tauc, P.2    Herve, G.3    Moody, M.F.4    Vachette, P.5
  • 22
    • 0035827220 scopus 로고    scopus 로고
    • The allosteric activator Mg-ATP modifies the quaternary structure of the R-state of Escherichia coli aspartate transcarbamylase without altering the T↔R equilibrium
    • Fetler L., Vachette P. The allosteric activator Mg-ATP modifies the quaternary structure of the R-state of Escherichia coli aspartate transcarbamylase without altering the T↔R equilibrium. J. Mol. Biol. 309:2001;817-832.
    • (2001) J. Mol. Biol. , vol.309 , pp. 817-832
    • Fetler, L.1    Vachette, P.2
  • 23
    • 0025328922 scopus 로고
    • Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenases by site-directed mutagenesis
    • Corbier C., Clermont S., Billard P., Skarzynski T., Branlant C., Wonacott A., Branlant G. Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenases by site-directed mutagenesis. Biochemistry. 29:1990;7101-7106.
    • (1990) Biochemistry , vol.29 , pp. 7101-7106
    • Corbier, C.1    Clermont, S.2    Billard, P.3    Skarzynski, T.4    Branlant, C.5    Wonacott, A.6    Branlant, G.7
  • 24
    • 0022787110 scopus 로고
    • Data appraisal, evaluation and display for synchrotron radiation experiments: Hardware and software
    • Boulin C., Kempf R., Koch M.H.J., McLaughlin S.M. Data appraisal, evaluation and display for synchrotron radiation experiments: hardware and software. Nucl. Instrum. Meth. A249:1986;399-407.
    • (1986) Nucl. Instrum. Meth. , vol.A249 , pp. 399-407
    • Boulin, C.1    Kempf, R.2    Koch, M.H.J.3    McLaughlin, S.M.4
  • 25
    • 0342511969 scopus 로고    scopus 로고
    • Improved signal-to-background ratio in small-angle X-ray scattering experiments with synchrotron radiation using an evacuated cell for solutions
    • Dubuisson J.M., Decamps T., Vachette P. Improved signal-to-background ratio in small-angle X-ray scattering experiments with synchrotron radiation using an evacuated cell for solutions. J. Appl. Crystallog. 30:1997;49-54.
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 49-54
    • Dubuisson, J.M.1    Decamps, T.2    Vachette, P.3
  • 27
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D.I., Barberato C., Koch M.H.J. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallog. 28:1995;768-773.
    • (1995) J. Appl. Crystallog. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3


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