메뉴 건너뛰기




Volumn 407, Issue 2, 2011, Pages 284-297

The crystal structures of eukaryotic phosphofructokinases from Baker's yeast and rabbit skeletal muscle

Author keywords

crystallography; fructose 2,6 bisphosphate; glycolysis; metabolism; protein structure

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; FRUCTOSE 2,6 BISPHOSPHATE; PHOSPHATE; SULFATE;

EID: 79952316682     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.01.019     Document Type: Article
Times cited : (44)

References (50)
  • 3
    • 0019751252 scopus 로고
    • Multimodulation of enzyme activity
    • Sols A. Multimodulation of enzyme activity Curr. Top. Cell. Regul. 19 1981 77 101
    • (1981) Curr. Top. Cell. Regul. , vol.19 , pp. 77-101
    • Sols, A.1
  • 4
    • 0023918674 scopus 로고
    • Hormonal regulation of hepatic gluconeogenesis and glycolysis
    • Pilkis S.J., El-Maghrabi M.R., and Claus T.H. Hormonal regulation of hepatic gluconeogenesis and glycolysis Annu. Rev. Biochem. 57 1988 755 783
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 755-783
    • Pilkis, S.J.1    El-Maghrabi, M.R.2    Claus, T.H.3
  • 5
    • 0032735328 scopus 로고    scopus 로고
    • Fructose-2,6-bisphosphate and control of carbohydrate metabolism in eukaryotes
    • Okar D.A., and Lange A.J. Fructose-2,6-bisphosphate and control of carbohydrate metabolism in eukaryotes Biofactors 10 1999 1 14 (Pubitemid 29500615)
    • (1999) BioFactors , vol.10 , Issue.1 , pp. 1-14
    • Okar, D.A.1    Lange, A.J.2
  • 6
    • 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 (Pubitemid 14102455)
    • (1984) Nature , vol.309 , Issue.5967 , pp. 467-469
    • Poorman, R.A.1    Randolph, A.2    Kemp, R.G.3    Heinrikson, R.L.4
  • 7
    • 0020574746 scopus 로고
    • A review of animal phosphofructokinase isozymes with an emphasis on their physiological role
    • Dunaway G.A. A review of animal phosphofructokinase isozymes with an emphasis on their physiological role Mol. Cell. Biochem. 52 1983 75 91 (Pubitemid 13065221)
    • (1983) Molecular and Cellular Biochemistry , vol.52 , Issue.1 , pp. 75-91
    • Dunaway, G.A.1
  • 8
    • 0016820219 scopus 로고
    • Electron microscope study of native and crosslinked rabbit muscle phosphofructokinase
    • Telford J.N., Lad P.M., and Hammes G.G. Electron microscope study of native and crosslinked rabbit muscle phosphofructokinase Proc. Natl Acad. Sci. USA 72 1975 3054 3056
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 3054-3056
    • Telford, J.N.1    Lad, P.M.2    Hammes, G.G.3
  • 9
    • 0019888384 scopus 로고
    • Structural properties of an active form of rabbit muscle phosphofructokinase
    • Hesterberg L.K., Lee J.C., and Erickson H.P. Structural properties of an active form of rabbit muscle phosphofructokinase J. Biol. Chem. 256 1981 9724 9730
    • (1981) J. Biol. Chem. , vol.256 , pp. 9724-9730
    • Hesterberg, L.K.1    Lee, J.C.2    Erickson, H.P.3
  • 10
    • 0040697064 scopus 로고    scopus 로고
    • Specific characteristics of phosphofructokinase-microtubule interactions
    • Vértessy B.G., Kovács J., and Ovádi J. Specific characteristics of phosphofructokinase-microtubule interactions FEBS Lett. 379 1996 191 195
    • (1996) FEBS Lett. , vol.379 , pp. 191-195
    • Vértessy, B.G.1    Kovács, J.2    Ovádi, J.3
  • 11
    • 4644249046 scopus 로고    scopus 로고
    • Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle
    • Silva A.P., Alves G.G., Araujo A.H., and Sola-Penna M. Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle An. Acad. Bras. Cienc. 76 2004 541 548 (Pubitemid 39288939)
    • (2004) Anais da Academia Brasileira de Ciencias , vol.76 , Issue.3 , pp. 541-548
    • Silva, A.P.P.1    Alves, G.G.2    Araujo, A.H.B.3    Sola-Penna, M.4
  • 13
    • 0017759685 scopus 로고
    • Physicochemical parameters and subunit composition of yeast phosphofructokinase
    • Kopperschläger G., Bär J., Nissler K., and Hofmann E. Physicochemical parameters and subunit composition of yeast phosphofructokinase Eur. J. Biochem. 81 1977 317 325 (Pubitemid 8241308)
    • (1977) European Journal of Biochemistry , vol.81 , Issue.2 , pp. 317-325
    • Kopperschlager, G.1    Bar, J.2    Nissler, K.3    Hofmann, E.4
  • 14
    • 0024358719 scopus 로고
    • The phosphofructokinase genes of yeast evolved from two duplication events
    • DOI 10.1016/0378-1119(89)90233-3
    • Heinisch J., Ritzel R.G., von Borstel R.C., Aguilera A., Rodicio R., and Zimmermann F.K. The phosphofructokinase genes of yeast evolved from two duplication events Gene 78 1989 309 321 (Pubitemid 19154209)
    • (1989) Gene , vol.78 , Issue.2 , pp. 309-321
    • Heinisch, J.1    Ritzel, R.G.2    Von Borstel, R.C.3    Aguilera, A.4    Rodicio, R.5    Zimmermann, F.K.6
  • 15
    • 0033534164 scopus 로고    scopus 로고
    • Identification of allosteric sites in rabbit phosphofracto-1-kinase
    • Li Y., Rivera D., Ru W., Gunasekera D., and Kemp R.G. Identification of allosteric sites in rabbit phosphofructo-1-kinase Biochemistry 38 1999 16407 16412 (Pubitemid 129520564)
    • (1999) Biochemistry , vol.38 , Issue.49 , pp. 16407-16412
    • Li, Y.1    Rivera, D.2    Ru, W.3    Gunasekera, D.4    Kemp, R.G.5
  • 16
    • 0018353474 scopus 로고
    • Structure and control of phosphofructokinase from Bacillus stearothermophilus
    • DOI 10.1038/279500a0
    • Evans P.R., and Hudson P.J. Structure and control of phosphofructokinase from Bacillus stearothermophilus Nature 279 1979 500 504 (Pubitemid 9195257)
    • (1979) Nature , vol.279 , Issue.5713 , pp. 500-504
    • Evans, P.R.1    Hudson, P.J.2
  • 18
    • 0024215739 scopus 로고
    • Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products
    • DOI 10.1016/0022-2836(88)90056-3
    • Shirakihara Y., and Evans P.R. Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products J. Mol. Biol. 204 1988 973 994 (Pubitemid 19050664)
    • (1988) Journal of Molecular Biology , vol.204 , Issue.4 , pp. 973-994
    • Shirakihara, Y.1    Evans, P.R.2
  • 19
    • 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 J. Mol. Biol. 207 1989 805 821
    • (1989) J. Mol. Biol. , vol.207 , pp. 805-821
    • Rypniewski, W.R.1    Evans, P.R.2
  • 20
    • 0025189804 scopus 로고
    • Structural basis of the allosteric behaviour of phosphofructokinase
    • Schirmer T., and Evans P.R. Structural basis of the allosteric behaviour of phosphofructokinase Nature 343 1990 140 145
    • (1990) Nature , vol.343 , pp. 140-145
    • Schirmer, T.1    Evans, P.R.2
  • 21
    • 0014028046 scopus 로고
    • Crystallization and properties of rabbit skeletal muscle phosphofructokinase
    • Parmeggiani A., Luft J.H., Love D.S., and Krebs E.G. Crystallization and properties of rabbit skeletal muscle phosphofructokinase J. Biol. Chem. 241 1966 4625 4637
    • (1966) J. Biol. Chem. , vol.241 , pp. 4625-4637
    • Parmeggiani, A.1    Luft, J.H.2    Love, D.S.3    Krebs, E.G.4
  • 22
    • 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 J. Struct. Biol. 136 2001 167 180
    • (2001) J. Struct. Biol. , vol.136 , pp. 167-180
    • Ruiz, T.1    Kopperschläger, G.2    Radermacher, M.3
  • 23
    • 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
    • DOI 10.1016/S1047-8477(03)00140-0
    • 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 J. Struct. Biol. 143 2003 124 134 (Pubitemid 37102960)
    • (2003) Journal of Structural Biology , vol.143 , Issue.2 , pp. 124-134
    • Ruiz, T.1    Mechin, I.2    Bar, J.3    Rypniewski, W.4    Kopperschlager, G.5    Radermacher, M.6
  • 24
    • 34249936593 scopus 로고    scopus 로고
    • The structure of the ATP-bound state of S. cerevisiae phosphofructokinase determined by cryo-electron microscopy
    • DOI 10.1016/j.jsb.2007.03.004, PII S1047847707000779
    • Bárcena M., Radermacher M., Bär J., Kopperschläger G., and Ruiz T. The structure of the ATP-bound state of S. cerevisiae phosphofructokinase determined by cryo-electron microscopy J. Struct. Biol. 159 2007 135 143 (Pubitemid 46880561)
    • (2007) Journal of Structural Biology , vol.159 , Issue.1 , pp. 135-143
    • Barcena, M.1    Radermacher, M.2    Bar, J.3    Kopperschlager, G.4    Ruiz, T.5
  • 26
    • 79251546410 scopus 로고    scopus 로고
    • Molecular architecture and structural basis of allosteric regulation of eukaryotic phosphofructokinases
    • Sträter N., Marek S., Kuettner E.B., Kloos M., Keim A., and Brüser A. Molecular architecture and structural basis of allosteric regulation of eukaryotic phosphofructokinases FASEB J. 25 2010 89 98
    • (2010) FASEB J. , vol.25 , pp. 89-98
    • Sträter, N.1    Marek, S.2    Kuettner, E.B.3    Kloos, M.4    Keim, A.5    Brüser, A.6
  • 28
    • 0027386009 scopus 로고
    • Limited proteolysis of yeast phosphofructokinase. Sequence locations of cleavage sites created by the actions of different proteinases
    • DOI 10.1111/j.1432-1033.1993.tb18273.x
    • Kopperschläger G., Bär J., and Stellwagen E. Limited proteolysis of yeast phosphofructokinase. Sequence locations of cleavage sites created by the actions of different proteinases Eur. J. Biochem. 217 1993 527 533 (Pubitemid 23311961)
    • (1993) European Journal of Biochemistry , vol.217 , Issue.2 , pp. 527-533
    • Kopperschlager, G.1    Bar, J.2    Stellwagen, E.3
  • 29
    • 0023654467 scopus 로고
    • Desensitization of muscle phosphofructokinase to ATP inhibition by removal of carboxyl-terminal heptadecapeptide
    • Valaitis A.P., Foe L.G., and Kemp R.G. Desensitization of muscle phosphofructokinase to ATP inhibition by removal of carboxyl-terminal heptadecapeptide J. Biol. Chem. 262 1987 5044 5048
    • (1987) J. Biol. Chem. , vol.262 , pp. 5044-5048
    • Valaitis, A.P.1    Foe, L.G.2    Kemp, R.G.3
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P.R. Scaling and assessment of data quality Acta Crystallogr. Sect. D 62 2006 72 82
    • (2006) Acta Crystallogr. Sect. D , vol.62 , pp. 72-82
    • Evans, P.R.1
  • 32
    • 0022552716 scopus 로고
    • Stereospecificity of the fructose 2,6-biphosphate site of muscle 6-phosphofructo-1-kinase
    • Kelley E.L., Voll R.J., Voll V.A., and Younathan E.S. Stereospecificity of the fructose 2,6-bisphosphate site of muscle 6-phosphofructo-1-kinase Biochemistry 25 1986 1245 1248 (Pubitemid 16048096)
    • (1986) Biochemistry , vol.25 , Issue.6 , pp. 1245-1248
    • Kelley, E.L.1    Voll, R.J.2    Voll, V.A.3    Younathan, E.S.4
  • 33
    • 0025065277 scopus 로고
    • Activation of mammalian phosphofructokinases by ribose 1,5-bisphosphate
    • Ishikawa E., Ogushi S., Ishikawa T., and Uyeda K. Activation of mammalian phosphofructokinases by ribose 1,5-bisphosphate J. Biol. Chem. 265 1990 18875 18878
    • (1990) J. Biol. Chem. , vol.265 , pp. 18875-18878
    • Ishikawa, E.1    Ogushi, S.2    Ishikawa, T.3    Uyeda, K.4
  • 34
    • 85047669951 scopus 로고
    • Allosteric regulatory properties of muscle phosphofructokinase
    • Kemp R.G., and Foe L.G. Allosteric regulatory properties of muscle phosphofructokinase (Review) Mol. Cell. Biochem. 57 1983 147 154 (Pubitemid 14205117)
    • (1983) Molecular and Cellular Biochemistry , vol.57 , Issue.2 , pp. 147-154
    • Kemp, R.G.1    Foe, L.G.2
  • 35
    • 0017096075 scopus 로고
    • Phosphofructokinase: I. Mechanism of the pH-dependent inactivation and reactivation of the rabbit muscle enzyme
    • Bock P.E., and Frieden C. Phosphofructokinase: I. Mechanism of the pH-dependent inactivation and reactivation of the rabbit muscle enzyme J. Biol. Chem. 251 1976 5630 5636
    • (1976) J. Biol. Chem. , vol.251 , pp. 5630-5636
    • Bock, P.E.1    Frieden, C.2
  • 36
    • 0027363656 scopus 로고
    • Site-directed mutagenesis of rabbit muscle phosphofructokinase cDNA. Mutations at glutamine 200 affect the allosteric properties of the enzyme
    • Li J., Zhu X., Byrnes M., Nelson J.W., and Chang S.H. Site-directed mutagenesis of rabbit muscle phosphofructokinase cDNA. Mutations at glutamine 200 affect the allosteric properties of the enzyme J. Biol. Chem. 268 1993 24599 24606 (Pubitemid 23335466)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.33 , pp. 24599-24606
    • Li, J.1    Zhu, X.2    Byrnes, M.3    Nelson, J.W.4    Chang, S.H.5
  • 37
    • 0036293409 scopus 로고    scopus 로고
    • Role of Ser530, Arg292, and His662 in the allosteric behavior of rabbit muscle phosphofructokinase
    • DOI 10.1006/bbrc.2001.6262
    • Chang S.H., and Kemp R.G. Role of Ser530, Arg292, and His662 in the allosteric behavior of rabbit muscle phosphofructokinase Biochem. Biophys. Res. Commun. 290 2002 670 675 (Pubitemid 34687492)
    • (2002) Biochemical and Biophysical Research Communications , vol.290 , Issue.2 , pp. 670-675
    • Chang, S.H.1    Kemp, R.G.2
  • 38
    • 66149151749 scopus 로고    scopus 로고
    • Subunit interactions and composition of the fructose 6-phosphate catalytic site and the fructose 2,6-bisphosphate allosteric site of mammalian phosphofructokinase
    • Ferreras C., Hernández E.D., Martínez-Costa O.H., and Aragón J.J. Subunit interactions and composition of the fructose 6-phosphate catalytic site and the fructose 2,6-bisphosphate allosteric site of mammalian phosphofructokinase J. Biol. Chem. 284 2009 9124 9131
    • (2009) J. Biol. Chem. , vol.284 , pp. 9124-9131
    • Ferreras, C.1    Hernández, E.D.2    Martínez-Costa, O.H.3    Aragón, J.J.4
  • 40
    • 0037199468 scopus 로고    scopus 로고
    • Evolution of the allosteric ligand sites of mammalian phosphofructo-1-kinase
    • DOI 10.1021/bi020110d
    • Kemp R.G., and Gunasekera D. Evolution of the allosteric sites of mammalian phosphofructo-1-kinase Biochemistry 41 2002 9426 9430 (Pubitemid 34810017)
    • (2002) Biochemistry , vol.41 , Issue.30 , pp. 9426-9430
    • Kemp, R.G.1    Gunasekera, D.2
  • 42
    • 0025381813 scopus 로고
    • Pdc1(0) mutants of Saccharomyces cerevisiae give evidence for an additional structural PDC gene: Cloning of PDC5, a gene homologous to PDC1
    • Seeboth P.G., Bohnsack K., and Hollenberg C.P. Pdc1(0) mutants of Saccharomyces cerevisiae give evidence for an additional structural PDC gene: cloning of PDC5, a gene homologous to PDC1 J. Bacteriol. 172 1990 678 685
    • (1990) J. Bacteriol. , vol.172 , pp. 678-685
    • Seeboth, P.G.1    Bohnsack, K.2    Hollenberg, C.P.3
  • 43
    • 0001954019 scopus 로고
    • Phosphofructokinase from baker's yeast: Properties of a proteolytically modified active enzyme form
    • Bär J., Huse K., Kopperschläger G., Behlke J., and Schultz W. Phosphofructokinase from baker's yeast: properties of a proteolytically modified active enzyme form Int. J. Biol. Macromol. 10 1988 99 105
    • (1988) Int. J. Biol. Macromol. , vol.10 , pp. 99-105
    • Bär, J.1    Huse, K.2    Kopperschläger, G.3    Behlke, J.4    Schultz, W.5
  • 44
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement Acta Crystallogr. Sect. A 50 1994 157 163
    • (1994) Acta Crystallogr. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 45
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. Sect. D 50 1994 760 763
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 46
    • 0002583957 scopus 로고
    • 'DM': An automated procedure for phase improvement by density modification
    • Cowtan K. 'DM': an automated procedure for phase improvement by density modification Jt. CCP4 ESF-EACBM Newsl. Protein Crystallogr. 31 1994 34 38
    • (1994) Jt. CCP4 ESF-EACBM Newsl. Protein Crystallogr. , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 49
    • 0037394492 scopus 로고    scopus 로고
    • A deliberate approach to screening for initial crystallization conditions of biological macromolecules
    • DOI 10.1016/S1047-8477(03)00048-0
    • Luft J.R., Collins J.R., Fehrman N.A., Lauricella A.M., Veatch C.K., and DeTitta G.T. A deliberate approach to screening for initial crystallizations of biological macromolecules J. Struct. Biol. 142 2003 170 179 (Pubitemid 36457899)
    • (2003) Journal of Structural Biology , vol.142 , Issue.1 , pp. 170-179
    • Luft, J.R.1    Collins, R.J.2    Fehrman, N.A.3    Lauricella, A.M.4    Veatch, C.K.5    DeTitta, G.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.