메뉴 건너뛰기




Volumn 159, Issue 1, 2007, Pages 135-143

The structure of the ATP-bound state of S. cerevisiae phosphofructokinase determined by cryo-electron microscopy

Author keywords

3D reconstruction; Eukaryotic enzyme; Glycolytic enzymes; Inhibited state; Point mode; Radon transforms; T state; X ray; Yeast

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; DIMER; FRUCTOSE 6 PHOSPHATE; TETRAMER;

EID: 34249936593     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2007.03.004     Document Type: Article
Times cited : (15)

References (40)
  • 1
    • 0001401503 scopus 로고
    • Phosphofructokinase from E. coli: evidence for a tetrameric structure of the enzyme
    • Blangy D. Phosphofructokinase from E. coli: evidence for a tetrameric structure of the enzyme. FEBS Letters 2 (1968) 109-111
    • (1968) FEBS Letters , vol.2 , pp. 109-111
    • Blangy, D.1
  • 2
    • 34249936737 scopus 로고    scopus 로고
    • Evans, P.R., 1992. Activity and Allosteric Regulation in Bacterial Phosphofructokinase. Regulation of Proteins by Ligands. Houston, Texas, pp. 39-54.
  • 3
    • 0022976785 scopus 로고
    • Crystallographic structure of allosterically inhibited phosphofructokinase at 7 Å resolution
    • Evans P.R., Farrants G.W., and Lawrence M.C. Crystallographic structure of allosterically inhibited phosphofructokinase at 7 Å resolution. Journal of Molecular Biology 191 (1986) 713-720
    • (1986) Journal of Molecular Biology , vol.191 , pp. 713-720
    • Evans, P.R.1    Farrants, G.W.2    Lawrence, M.C.3
  • 4
    • 0018353474 scopus 로고
    • Structure and control of phosphofructokinase from Bacillus stearothermophilus
    • Evans P.R., and Hudson P.J. Structure and control of phosphofructokinase from Bacillus stearothermophilus. Nature 279 (1979) 500-504
    • (1979) Nature , vol.279 , pp. 500-504
    • Evans, P.R.1    Hudson, P.J.2
  • 6
    • 0022595650 scopus 로고
    • Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast
    • Heinisch J. Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast. Molecular and General Genetics 202 (1986) 75-82
    • (1986) Molecular and General Genetics , vol.202 , pp. 75-82
    • Heinisch, J.1
  • 10
    • 0027386009 scopus 로고
    • Limited proteolysis of yeast phosphofructokinase. Sequence locations of cleavage sites created by the actions of different proteinases
    • Kopperschläger G., Bär J., and Stellwagen E. Limited proteolysis of yeast phosphofructokinase. Sequence locations of cleavage sites created by the actions of different proteinases. European Journal of Biochemistry 217 (1993) 527-533
    • (1993) European Journal of Biochemistry , vol.217 , pp. 527-533
    • Kopperschläger, G.1    Bär, J.2    Stellwagen, E.3
  • 11
    • 0032938975 scopus 로고    scopus 로고
    • Phosphofructokinase-1 from Saccharomyces cerevisiae: analysis of molecular structure and function by electron microscopy and self-catalysed affinity labelling
    • Kricke J., Mayer F., Kopperschläger G., and Kriegel T. Phosphofructokinase-1 from Saccharomyces cerevisiae: analysis of molecular structure and function by electron microscopy and self-catalysed affinity labelling. International Journal of Biological Macromolecules 24 (1999) 27-35
    • (1999) International Journal of Biological Macromolecules , vol.24 , pp. 27-35
    • Kricke, J.1    Mayer, F.2    Kopperschläger, G.3    Kriegel, T.4
  • 13
    • 0018801321 scopus 로고
    • Allosteric regulation of yeast phosphofructokinase. Correlation between equilibrium binding, spectroscopic and kinetic data
    • Laurent M., Seydoux F.J., and Dessen P. Allosteric regulation of yeast phosphofructokinase. Correlation between equilibrium binding, spectroscopic and kinetic data. Journal of Biological Chemistry 254 (1979) 7515-7520
    • (1979) Journal of Biological Chemistry , vol.254 , pp. 7515-7520
    • Laurent, M.1    Seydoux, F.J.2    Dessen, P.3
  • 14
    • 0021321701 scopus 로고
    • Solution X-ray scattering studies of the yeast phosphofructokinase allosteric transition. Characterization of an ATP-induced conformation distinct in quaternary structure from the R and T states of the enzyme
    • Laurent M., Tijane M.N., Roucous C., Seydoux F.J., and Tardieu A. Solution X-ray scattering studies of the yeast phosphofructokinase allosteric transition. Characterization of an ATP-induced conformation distinct in quaternary structure from the R and T states of the enzyme. Journal of Biological Chemistry 259 (1984) 3124-3126
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 3124-3126
    • Laurent, M.1    Tijane, M.N.2    Roucous, C.3    Seydoux, F.J.4    Tardieu, A.5
  • 15
    • 34249936839 scopus 로고    scopus 로고
    • Mechin, I., 2002. Crystal Structure of Fructose-6-Phosphate Liganded R-State 6-Phosphofructo-1-Kinase from Saccharomyces cerevisiae at 2.9 Å Resolution. Ph.D. Thesis, Department of Biochemistry, Leipzig University.
  • 20
    • 0017886457 scopus 로고
    • Small-angle x-ray scattering studies on the quaternary structure of phosphofructokinase from baker's yeast
    • Plietz P., Damaschun G., Kopperschläger G., and Müller J.J. Small-angle x-ray scattering studies on the quaternary structure of phosphofructokinase from baker's yeast. FEBS Letters 91 (1978) 230-232
    • (1978) FEBS Letters , vol.91 , pp. 230-232
    • Plietz, P.1    Damaschun, G.2    Kopperschläger, G.3    Müller, J.J.4
  • 21
    • 0021256418 scopus 로고
    • Evolution of phosphofructokinase-gene duplication and creation of new effector sites
    • Poorman R.A., Randolph A., Kemp R.G., and Heinrikson R.L. Evolution of phosphofructokinase-gene duplication and creation of new effector sites. Nature 309 (1984) 467-469
    • (1984) Nature , vol.309 , pp. 467-469
    • Poorman, R.A.1    Randolph, A.2    Kemp, R.G.3    Heinrikson, R.L.4
  • 22
    • 0028375920 scopus 로고
    • Three-dimensional reconstruction from random projections: orientational alignment via Radon transforms
    • Radermacher M. Three-dimensional reconstruction from random projections: orientational alignment via Radon transforms. Ultramicroscopy 53 (1994) 121-136
    • (1994) Ultramicroscopy , vol.53 , pp. 121-136
    • Radermacher, M.1
  • 23
    • 0001090508 scopus 로고    scopus 로고
    • Radon transform techniques for alignment and 3D reconstruction from random projections
    • Radermacher M. Radon transform techniques for alignment and 3D reconstruction from random projections. Scanning Microscopy 11 (1997) 171-177
    • (1997) Scanning Microscopy , vol.11 , pp. 171-177
    • Radermacher, M.1
  • 24
    • 0011909229 scopus 로고    scopus 로고
    • Appendix: simultaneous rotational and translational alignment
    • Radermacher M. Appendix: simultaneous rotational and translational alignment. Journal of Structural Biology 135 (2001) 35-37
    • (2001) Journal of Structural Biology , vol.135 , pp. 35-37
    • Radermacher, M.1
  • 25
    • 33747410587 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of single particles in electron microscopy image processing
    • Radermacher M., and Ruiz T. Three-dimensional reconstruction of single particles in electron microscopy image processing. Methods in Molecular Biology 319 (2006) 427-461
    • (2006) Methods in Molecular Biology , vol.319 , pp. 427-461
    • Radermacher, M.1    Ruiz, T.2
  • 27
    • 0035782681 scopus 로고    scopus 로고
    • The structure of the V1-ATPase determined by three-dimensional electron microscopy of single particles
    • Radermacher M., Ruiz T., Wieczorek H., and Grüber G. The structure of the V1-ATPase determined by three-dimensional electron microscopy of single particles. Journal of structural biology 135 (2001) 26-37
    • (2001) Journal of structural biology , vol.135 , pp. 26-37
    • Radermacher, M.1    Ruiz, T.2    Wieczorek, H.3    Grüber, G.4
  • 29
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal P.B., and Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. Journal of Molecular Biology 333 (2003) 721-745
    • (2003) Journal of Molecular Biology , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 30
    • 0035782688 scopus 로고    scopus 로고
    • The first three-dimensional structure of phosphofructokinase from Saccharomyces cerevisiae determined by electron microscopy of single particles
    • Ruiz T., Kopperschläger G., and Radermacher M. The first three-dimensional structure of phosphofructokinase from Saccharomyces cerevisiae determined by electron microscopy of single particles. Journal of Structural Biology 136 (2001) 167-180
    • (2001) Journal of Structural Biology , vol.136 , pp. 167-180
    • Ruiz, T.1    Kopperschläger, G.2    Radermacher, M.3
  • 31
    • 0041334007 scopus 로고    scopus 로고
    • The 10.8 Å structure of Saccharomyces cerevisiae phosphofructokinase determined by cryoelectron microscopy: localization of the putative fructose 6-phosphate binding sites
    • Ruiz T., Mechin I., Bär J., Rypniewski W., Kopperschläger G., and Radermacher M. The 10.8 Å structure of Saccharomyces cerevisiae phosphofructokinase determined by cryoelectron microscopy: localization of the putative fructose 6-phosphate binding sites. Journal of Structural Biology 143 (2003) 124-134
    • (2003) Journal of Structural Biology , vol.143 , pp. 124-134
    • Ruiz, T.1    Mechin, I.2    Bär, J.3    Rypniewski, W.4    Kopperschläger, G.5    Radermacher, M.6
  • 32
    • 33747421767 scopus 로고    scopus 로고
    • Three-dimensional analysis of single particles by electron microscopy: sample preparation and data acquisition
    • Ruiz T., and Radermacher M. Three-dimensional analysis of single particles by electron microscopy: sample preparation and data acquisition. Methods in Molecular Biology 319 (2006) 403-425
    • (2006) Methods in Molecular Biology , vol.319 , pp. 403-425
    • Ruiz, T.1    Radermacher, M.2
  • 33
    • 0024974796 scopus 로고
    • Crystal structure of unliganded phosphofructokinase from Escherichia coli
    • Rypniewski W.R., and Evans P.R. Crystal structure of unliganded phosphofructokinase from Escherichia coli. Journal of Molecular Biology 207 (1989) 805-821
    • (1989) Journal of Molecular Biology , vol.207 , pp. 805-821
    • Rypniewski, W.R.1    Evans, P.R.2
  • 34
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • Saxton W.O., and Baumeister W. The correlation averaging of a regularly arranged bacterial cell envelope protein. Journal of Microscopy 127 (1982) 127-138
    • (1982) Journal of Microscopy , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 35
    • 0024215739 scopus 로고
    • Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products
    • Shirakihara Y., and Evans P.R. Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products. Journal of Molecular Biology 204 (1988) 973-994
    • (1988) Journal of Molecular Biology , vol.204 , pp. 973-994
    • Shirakihara, Y.1    Evans, P.R.2
  • 37
    • 0016701561 scopus 로고
    • Limited proteolysis of yeast phosphofructokinase by subtilisin. Alterations in enzyme activity, subunit composition, and hydrodynamic properties
    • Taucher M., Kopperschläger G., and Hofmann E. Limited proteolysis of yeast phosphofructokinase by subtilisin. Alterations in enzyme activity, subunit composition, and hydrodynamic properties. European Journal of Biochemistry 59 (1975) 319-325
    • (1975) European Journal of Biochemistry , vol.59 , pp. 319-325
    • Taucher, M.1    Kopperschläger, G.2    Hofmann, E.3
  • 38
    • 0018792350 scopus 로고
    • Octameric structure of yeast phosphofructokinase as determined by crosslinking with disuccinimidyl beta-hydromuconate
    • Tijane M.N., Seydoux F.J., Hill M., Roucous C., and Laurent M. Octameric structure of yeast phosphofructokinase as determined by crosslinking with disuccinimidyl beta-hydromuconate. FEBS Letters 105 (1979) 249-253
    • (1979) FEBS Letters , vol.105 , pp. 249-253
    • Tijane, M.N.1    Seydoux, F.J.2    Hill, M.3    Roucous, C.4    Laurent, M.5
  • 39
    • 34249930247 scopus 로고    scopus 로고
    • van Heel, M., Keegstra, W., Schutter, W., Bruggen, E.J.F., 1982. Arthropod hemocyanin structures studied by image analysis. In: J., W.E. (Ed), Life Chemistry Reports, Suppl. 1, The structure and Function of Invertebrate Respiratory Proteins. Embo Workshop, pp. 69-73.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.