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Volumn 366, Issue 4, 2007, Pages 1185-1198

The First Crystal Structure of Phosphofructokinase from a Eukaryote: Trypanosoma brucei

Author keywords

eukaryote; phosphofructokinase; structure based drug discovery; Trypanosoma brucei; X ray crystallography

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME;

EID: 33846806104     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.10.019     Document Type: Article
Times cited : (24)

References (39)
  • 2
    • 0017366999 scopus 로고
    • Localization of nine glycolytic enzymes in a microbody-like organelle in Trypanosoma brucei: the glycosome
    • Opperdoes F.R., and Borst P. Localization of nine glycolytic enzymes in a microbody-like organelle in Trypanosoma brucei: the glycosome. FEBS Letters 80 (1977) 360-364
    • (1977) FEBS Letters , vol.80 , pp. 360-364
    • Opperdoes, F.R.1    Borst, P.2
  • 3
    • 0018945812 scopus 로고
    • Trypanosoma brucei - activities and subcellular distribution of glycolytic enzymes from differently disrupted cells
    • Oduro K.K., Flynn I.E., and Bowman I.B.R. Trypanosoma brucei - activities and subcellular distribution of glycolytic enzymes from differently disrupted cells. Expt. Parasitol. 50 (1980) 123-135
    • (1980) Expt. Parasitol. , vol.50 , pp. 123-135
    • Oduro, K.K.1    Flynn, I.E.2    Bowman, I.B.R.3
  • 5
    • 0031574041 scopus 로고    scopus 로고
    • The glycosomal ATP-dependent phosphofructokinase of Trypanosoma brucei must have evolved from an ancestral pyrophosphate-dependent enzyme
    • Michels P.A.M., Chevalier N., Opperdoes F.R., Rider M.H., and Rigden D.J. The glycosomal ATP-dependent phosphofructokinase of Trypanosoma brucei must have evolved from an ancestral pyrophosphate-dependent enzyme. Eur. J. Biochem. 250 (1997) 698-704
    • (1997) Eur. J. Biochem. , vol.250 , pp. 698-704
    • Michels, P.A.M.1    Chevalier, N.2    Opperdoes, F.R.3    Rider, M.H.4    Rigden, D.J.5
  • 6
    • 0036038938 scopus 로고    scopus 로고
    • Leishmania donovani phosphofructokinase: gene characterization, biochemical properties and structure-modelling studies
    • López C., Chevalier N., Hannaert V., Rigden D.J., Michels P.A.M., and Ramirez J.L. Leishmania donovani phosphofructokinase: gene characterization, biochemical properties and structure-modelling studies. Eur. J. Biochem. 269 (2002) 3978-3989
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3978-3989
    • López, C.1    Chevalier, N.2    Hannaert, V.3    Rigden, D.J.4    Michels, P.A.M.5    Ramirez, J.L.6
  • 7
    • 0021883206 scopus 로고
    • Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase
    • Hellinga H.W., and Evans P.J. Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase. Eur. J. Biochem. 149 (1985) 363-373
    • (1985) Eur. J. Biochem. , vol.149 , pp. 363-373
    • Hellinga, H.W.1    Evans, P.J.2
  • 8
    • 0020574746 scopus 로고
    • A review of animal phosphofructokinase isoenzymes with an emphasis on their physiological role
    • Dunaway G.A. A review of animal phosphofructokinase isoenzymes with an emphasis on their physiological role. Mol. Cell Biol. 52 (1983) 75-91
    • (1983) Mol. Cell Biol. , vol.52 , pp. 75-91
    • Dunaway, G.A.1
  • 9
    • 0021256418 scopus 로고
    • Evolution of phosphofructokinase: gene duplication and creation of new effector sites
    • Poorman R.A., Randolph A., Kemp R.G., and Henrikson 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    Henrikson, R.L.4
  • 10
    • 0020108137 scopus 로고
    • Regulation of glycolysis in Trypanosoma brucei: hexokinase and phosphofructokinase activity
    • Nwagwu M., and Opperdoes F.R. Regulation of glycolysis in Trypanosoma brucei: hexokinase and phosphofructokinase activity. Acta Tropica 39 (1982) 61-72
    • (1982) Acta Tropica , vol.39 , pp. 61-72
    • Nwagwu, M.1    Opperdoes, F.R.2
  • 11
    • 0021874922 scopus 로고
    • Purification and regulatory properties of phosphofructokinase from Trypanosoma (Trypanozoon) brucei brucei
    • Cronin C.N., and Tipton K.F. Purification and regulatory properties of phosphofructokinase from Trypanosoma (Trypanozoon) brucei brucei. Biochem. J. 227 (1985) 113-124
    • (1985) Biochem. J. , vol.227 , pp. 113-124
    • Cronin, C.N.1    Tipton, K.F.2
  • 12
    • 0023374587 scopus 로고
    • Kinetic studies on the reaction catalysed by phosphofructokinase from Trypanosoma brucei
    • Cronin C.N., and Tipton K.F. Kinetic studies on the reaction catalysed by phosphofructokinase from Trypanosoma brucei. Biochem. J. 245 (1987) 13-18
    • (1987) Biochem. J. , vol.245 , pp. 13-18
    • Cronin, C.N.1    Tipton, K.F.2
  • 16
    • 0036094071 scopus 로고    scopus 로고
    • The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi
    • Moore S.A., Ronimus R.S., Roberson R.S., and Morgan H.W. The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi. Structure 10 (2002) 659-671
    • (2002) Structure , vol.10 , pp. 659-671
    • Moore, S.A.1    Ronimus, R.S.2    Roberson, R.S.3    Morgan, H.W.4
  • 18
    • 0022264053 scopus 로고
    • Cross-linking of the enzymes in the glycosome of Trypanosoma brucei
    • Aman R.A., Kenyon G.L., and Wang C.C. Cross-linking of the enzymes in the glycosome of Trypanosoma brucei. J. Biol. Chem. 260 (1985) 6966-6973
    • (1985) J. Biol. Chem. , vol.260 , pp. 6966-6973
    • Aman, R.A.1    Kenyon, G.L.2    Wang, C.C.3
  • 19
    • 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. Mol. Gen. Genet. 202 (1986) 75-82
    • (1986) Mol. Gen. Genet. , vol.202 , pp. 75-82
    • Heinisch, J.1
  • 20
    • 0032429638 scopus 로고    scopus 로고
    • The pyrophosphate-dependent phosphofructokinase of the protist, Trichomonas vaginalis, and the evolutionary relationships of protist phosphofructokinases
    • Mertens E., Ladror U.S., Lee J.A., Miretsky A., Morris A., Rozario C., et al. The pyrophosphate-dependent phosphofructokinase of the protist, Trichomonas vaginalis, and the evolutionary relationships of protist phosphofructokinases. J. Mol. Evol. 47 (1998) 739-750
    • (1998) J. Mol. Evol. , vol.47 , pp. 739-750
    • Mertens, E.1    Ladror, U.S.2    Lee, J.A.3    Miretsky, A.4    Morris, A.5    Rozario, C.6
  • 22
    • 0041955200 scopus 로고    scopus 로고
    • Rampant horizontal gene transfer and phospho-donor change in the evolution of the phosphofructokinase
    • Bapteste E., Moreira D., and Philippe H. Rampant horizontal gene transfer and phospho-donor change in the evolution of the phosphofructokinase. Gene 318 (2003) 185-191
    • (2003) Gene , vol.318 , pp. 185-191
    • Bapteste, E.1    Moreira, D.2    Philippe, H.3
  • 23
    • 0034680770 scopus 로고    scopus 로고
    • The primordial high-energy compound: ATP or inorganic pyrophosphate?
    • Chi A., and Kemp R.G. The primordial high-energy compound: ATP or inorganic pyrophosphate?. J. Biol. Chem. 275 (2000) 35677-35679
    • (2000) J. Biol. Chem. , vol.275 , pp. 35677-35679
    • Chi, A.1    Kemp, R.G.2
  • 24
    • 0033534164 scopus 로고    scopus 로고
    • Identification of allosteric sites in rabbit phosphofructo-1-kinase
    • Li Y.L., Rivera D., Ru W., Gunasekera D., and Kemp R.G. Identification of allosteric sites in rabbit phosphofructo-1-kinase. Biochemistry 38 (1999) 16407-16412
    • (1999) Biochemistry , vol.38 , pp. 16407-16412
    • Li, Y.L.1    Rivera, D.2    Ru, W.3    Gunasekera, D.4    Kemp, R.G.5
  • 25
    • 0037199468 scopus 로고    scopus 로고
    • Evolution of the allosteric ligand sites of mammalian phosphofructo-1-kinase
    • Kemp R.G., and Gunasekera D. Evolution of the allosteric ligand sites of mammalian phosphofructo-1-kinase. Biochemistry 41 (2002) 9426-9430
    • (2002) Biochemistry , vol.41 , pp. 9426-9430
    • Kemp, R.G.1    Gunasekera, D.2
  • 26
    • 33846833402 scopus 로고    scopus 로고
    • Nowicki, M. W. (2005). Development of lead compounds for trypanocidal drugs based on inhibitors of parasite glycolysis. PhD thesis, University of Edinburgh.
  • 27
    • 0033528726 scopus 로고    scopus 로고
    • Identification of residues of Escherichia coli phosphofructokinase that contribute to nucleotide binding and specificity
    • Wang X., and Kemp R.G. Identification of residues of Escherichia coli phosphofructokinase that contribute to nucleotide binding and specificity. Biochemistry 38 (1999) 4313-4318
    • (1999) Biochemistry , vol.38 , pp. 4313-4318
    • Wang, X.1    Kemp, R.G.2
  • 28
    • 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
  • 29
    • 0019321863 scopus 로고
    • Quaternary structure of pig liver phosphofructokinase
    • Foe L.G., and Trujillo J.L. Quaternary structure of pig liver phosphofructokinase. J. Biol. Chem. 255 (1980) 10537-10541
    • (1980) J. Biol. Chem. , vol.255 , pp. 10537-10541
    • Foe, L.G.1    Trujillo, J.L.2
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 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 Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 33
    • 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. J. Mol. Biol. 204 (1988) 973-994
    • (1988) J. Mol. Biol. , vol.204 , pp. 973-994
    • Shirakihara, Y.1    Evans, P.R.2
  • 35
    • 0030852350 scopus 로고    scopus 로고
    • Automated refinement for protein crystallography
    • Lamzin V.S., and Wilson K.S. Automated refinement for protein crystallography. Methods Enzymol. 277 (1997) 269-305
    • (1997) Methods Enzymol. , vol.277 , pp. 269-305
    • Lamzin, V.S.1    Wilson, K.S.2
  • 36
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins D., Thompson J., Gibson T., Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22 (1994) 4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 38
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 39
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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