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Volumn 19, Issue 7, 2000, Pages 1419-1431

Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus

Author keywords

Bacillus stearothermophilus; Mechanism; Phosphoglycerate mutase; Spores; Structure

Indexed keywords

2,3 DIPHOSPHOGLYCERIC ACID; MANGANESE; PHOSPHATE; PHOSPHOGLYCERATE MUTASE; PHOSPHOSERINE; PHOSPHOTRANSFERASE; SERINE;

EID: 0034599751     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.7.1419     Document Type: Article
Times cited : (77)

References (43)
  • 1
    • 0011555439 scopus 로고
    • Tertiary structure modeling of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: Structural, functional and evolutionary design of a bifunctional enzyme
    • Pilkis, S.J. (ed.). CRC Press, Boca Raton, FL
    • Bazan, J.F. and Fletterrick, R.J. (1990) Tertiary structure modeling of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: structural, functional and evolutionary design of a bifunctional enzyme. In Pilkis, S.J. (ed.), Fructose 2,6-Bisphosphate. CRC Press, Boca Raton, FL, pp. 125-171.
    • (1990) Fructose 2,6-Bisphosphate , pp. 125-171
    • Bazan, J.F.1    Fletterrick, R.J.2
  • 2
    • 0019328525 scopus 로고
    • Phosphoglycerate mutases: Stereochemical course of the phosphoryl group transfers catalyzed by the cofactor-dependent enzyme from rabbit muscle and the cofactor-independent enzyme from wheat germ
    • Blatter, A.W. and Knowles, J.R. (1980) Phosphoglycerate mutases: stereochemical course of the phosphoryl group transfers catalyzed by the cofactor-dependent enzyme from rabbit muscle and the cofactor-independent enzyme from wheat germ. Biochemistry, 19, 738-743.
    • (1980) Biochemistry , vol.19 , pp. 738-743
    • Blatter, A.W.1    Knowles, J.R.2
  • 3
    • 0017401334 scopus 로고
    • 18O-labeled substrate, investigations of the phosphatase and phosphoryl transfer activities and evidence for a phosphoryl-enzyme intermediate
    • 18O-labeled substrate, investigations of the phosphatase and phosphoryl transfer activities and evidence for a phosphoryl-enzyme intermediate. Biochemistry, 16, 3054-3060.
    • (1977) Biochemistry , vol.16 , pp. 3054-3060
    • Breathnach, R.1    Knowles, J.R.2
  • 4
    • 0015237758 scopus 로고
    • Mechanism of action of 2,3-diphosphoglycerate-independent phosphoglycerate mutase
    • Britton, H.G., Carrerras, J. and Grisolia, S. (1971) Mechanism of action of 2,3-diphosphoglycerate-independent phosphoglycerate mutase. Biochemistry, 10, 4522-4533.
    • (1971) Biochemistry , vol.10 , pp. 4522-4533
    • Britton, H.G.1    Carrerras, J.2    Grisolia, S.3
  • 6
    • 0016327034 scopus 로고
    • Structure of yeast phosphoglycerate mutase
    • Campbell, J.W., Watson, H.C. and Hodgson, G.I. (1974) Structure of yeast phosphoglycerate mutase. Nature, 250, 301-303.
    • (1974) Nature , vol.250 , pp. 301-303
    • Campbell, J.W.1    Watson, H.C.2    Hodgson, G.I.3
  • 7
    • 0020020251 scopus 로고
    • Phylogeny and ontogeny of the phosphoglycerate mutases-IV. Distribution of glycerate-2,3-P2 dependent and independent phosphoglycerate mutases in algae, fungi, plants and animals
    • Carreras, J., Mezquita, J., Bosch, J., Bartrons, R. and Pons, G. (1982) Phylogeny and ontogeny of the phosphoglycerate mutases-IV. Distribution of glycerate-2,3-P2 dependent and independent phosphoglycerate mutases in algae, fungi, plants and animals. Comp. Biochem. Physiol. B, 71, 591-597.
    • (1982) Comp. Biochem. Physiol. B , vol.71 , pp. 591-597
    • Carreras, J.1    Mezquita, J.2    Bosch, J.3    Bartrons, R.4    Pons, G.5
  • 8
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson, M.J. (1987) Ribbon models of macromolecules. J. Mol. Graph., 5, 103-106.
    • (1987) J. Mol. Graph. , vol.5 , pp. 103-106
    • Carson, M.J.1
  • 10
    • 0033563772 scopus 로고    scopus 로고
    • Structural studies on a 2,3-diphosphoglycerate independent phosphoglycerate mutase from Bacillus stearothermophilus
    • Chander, M., Setlow, P., Lamani, E. and Jedrzejas, M.J. (1999) Structural studies on a 2,3-diphosphoglycerate independent phosphoglycerate mutase from Bacillus stearothermophilus. J. Struct. Biol., 126, 156-165.
    • (1999) J. Struct. Biol. , vol.126 , pp. 156-165
    • Chander, M.1    Setlow, P.2    Lamani, E.3    Jedrzejas, M.J.4
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D, 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 12
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. (1997) An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph., 15, 133-138.
    • (1997) J. Mol. Graph. , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 14
    • 0032815379 scopus 로고    scopus 로고
    • The two analogous phosphoglycerate mutases of Escherichia coli
    • Fraser, H.I., Kratskhelia, M. and White, M.F. (1999) The two analogous phosphoglycerate mutases of Escherichia coli. FEBS Lett., 455, 344-348.
    • (1999) FEBS Lett. , vol.455 , pp. 344-348
    • Fraser, H.I.1    Kratskhelia, M.2    White, M.F.3
  • 15
    • 0032461412 scopus 로고    scopus 로고
    • A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases
    • Galperin, M.Y., Bairoch, A. and Koonin, E.V. (1998) A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. Protein Sci., 7, 1829-1835.
    • (1998) Protein Sci. , vol.7 , pp. 1829-1835
    • Galperin, M.Y.1    Bairoch, A.2    Koonin, E.V.3
  • 16
    • 0017377181 scopus 로고
    • Phosphoglycerate mutase from wheat germ: Studies with isotopically labeled 3-phospho-D-glycerates showing that the catalyzed reaction is intramolecular
    • Gatehouse, J.A. and Knowles, J.R. (1977) Phosphoglycerate mutase from wheat germ: studies with isotopically labeled 3-phospho-D-glycerates showing that the catalyzed reaction is intramolecular. Biochemistry, 16, 3045-3050.
    • (1977) Biochemistry , vol.16 , pp. 3045-3050
    • Gatehouse, J.A.1    Knowles, J.R.2
  • 18
    • 0033179802 scopus 로고    scopus 로고
    • The geometry of metal-ligand interactions relevant to proteins
    • Harding, M.M. (1999) The geometry of metal-ligand interactions relevant to proteins. Acta Crystallogr. D, 55, 1432-1443.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1432-1443
    • Harding, M.M.1
  • 19
    • 0028232955 scopus 로고
    • Searching protein structure data bases has come of age
    • Holm, L. and Sander, C. (1994) Searching protein structure data bases has come of age. Proteins, 19, 165-173.
    • (1994) Proteins , vol.19 , pp. 165-173
    • Holm, L.1    Sander, C.2
  • 20
    • 85047691165 scopus 로고
    • Histidine residues 139, 363 and 500 are essential for catalytic activity of cofactor-independent phosphoglyceromutase from developing endosperm of the castor plant
    • Huang, Y. and Dennis, D.T. (1995) Histidine residues 139, 363 and 500 are essential for catalytic activity of cofactor-independent phosphoglyceromutase from developing endosperm of the castor plant. Eur. J. Biochem., 229, 395-402.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 395-402
    • Huang, Y.1    Dennis, D.T.2
  • 21
    • 0024287779 scopus 로고
    • Do metal ions promote the reactivation of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutases?
    • Johnson, M. and Price, N.C. (1988) Do metal ions promote the reactivation of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutases? Biochem. J., 252, 111-117.
    • (1988) Biochem. J. , vol.252 , pp. 111-117
    • Johnson, M.1    Price, N.C.2
  • 22
    • 0029962708 scopus 로고    scopus 로고
    • Structure of a unique binuclear manganese cluster in arginase
    • Kanyo, Z.F., Scolnick, L.R., Ash, D.E. and Christianson, D.W. (1996) Structure of a unique binuclear manganese cluster in arginase. Nature, 383, 554-557.
    • (1996) Nature , vol.383 , pp. 554-557
    • Kanyo, Z.F.1    Scolnick, L.R.2    Ash, D.E.3    Christianson, D.W.4
  • 23
    • 0025814510 scopus 로고
    • pH-sensitive control of arginase by Mn(II) ions at submicromolar concentrations
    • Kuhn, N.J., Talbot, J. and Ward, S. (1991) pH-sensitive control of arginase by Mn(II) ions at submicromolar concentrations. Arch. Biochem. Biophys., 286, 217-221.
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 217-221
    • Kuhn, N.J.1    Talbot, J.2    Ward, S.3
  • 24
    • 0029050373 scopus 로고
    • Cooperative manganese(II) activation of 3-phosphoglycerate mutase of Bacillus megaterium. A biological pH-sensing mechanism in bacterial spore formation and germination
    • Kuhn, N.J., Setlow, B., Setlow, P., Cammack, R. and Williams, R. (1995) Cooperative manganese(II) activation of 3-phosphoglycerate mutase of Bacillus megaterium. A biological pH-sensing mechanism in bacterial spore formation and germination. Arch. Biochem. Biophys., 320, 35-42.
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 35-42
    • Kuhn, N.J.1    Setlow, B.2    Setlow, P.3    Cammack, R.4    Williams, R.5
  • 25
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. and Wilson, K.S. (1993) Automated refinement of protein models. Acta Crystallogr. D, 49, 129-147.
    • (1993) Acta Crystallogr. D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 26
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical qualities of protein structures
    • Laskowski, R., Macarthur, M., Moss, D. and Thornton, J. (1993) PROCHECK: a program to check the stereochemical qualities of protein structures. J. Appl. Crystallogr., 26, 283-290.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-290
    • Laskowski, R.1    Macarthur, M.2    Moss, D.3    Thornton, J.4
  • 27
    • 0028224273 scopus 로고
    • The internal pH of the forespore compartment of Bacillus megaterium decreases by about 1 pH unit during sporulation
    • Magill, N.G., Cowan, A.E., Koppel, D.E. and Setlow, P. (1994) The internal pH of the forespore compartment of Bacillus megaterium decreases by about 1 pH unit during sporulation. J. Bacteriol., 178, 2252-2258.
    • (1994) J. Bacteriol. , vol.178 , pp. 2252-2258
    • Magill, N.G.1    Cowan, A.E.2    Koppel, D.E.3    Setlow, P.4
  • 28
    • 0029974595 scopus 로고    scopus 로고
    • Analysis of the relationship between the decrease in pH and accumulation of 3-phosphoglyceric acid in developing forespores of Bacillus species
    • Magill, N.G., Cowan, A.E., Leyva-Vazquez, M.A., Brown, M., Koppel, D.E. and Setlow, P. (1996) Analysis of the relationship between the decrease in pH and accumulation of 3-phosphoglyceric acid in developing forespores of Bacillus species. J. Bacteriol., 178, 2204-2210.
    • (1996) J. Bacteriol. , vol.178 , pp. 2204-2210
    • Magill, N.G.1    Cowan, A.E.2    Leyva-Vazquez, M.A.3    Brown, M.4    Koppel, D.E.5    Setlow, P.6
  • 29
    • 0013833140 scopus 로고
    • Metal ion interactions and glutamine synthetase activity
    • Monder, C. (1965) Metal ion interactions and glutamine synthetase activity. Biochemistry, 4, 2677-2686.
    • (1965) Biochemistry , vol.4 , pp. 2677-2686
    • Monder, C.1
  • 30
    • 0028897146 scopus 로고
    • The use of mass spectrometry to examine the phosphorylation and hydrolysis of the phosphorylated form of phosphoglycerate mutase
    • Nairn, J.N., Krell, T., Coggins, J.R., Pitt, A.R., Fothergill-Gilmore, L.A., Walter, R. and Price, N.N. (1995) The use of mass spectrometry to examine the phosphorylation and hydrolysis of the phosphorylated form of phosphoglycerate mutase. FEBS Lett., 359, 192-194.
    • (1995) FEBS Lett. , vol.359 , pp. 192-194
    • Nairn, J.N.1    Krell, T.2    Coggins, J.R.3    Pitt, A.R.4    Fothergill-Gilmore, L.A.5    Walter, R.6    Price, N.N.7
  • 31
  • 32
    • 0015119977 scopus 로고
    • The phosphorylation of yeast phosphoglycerate mutase
    • Rose, Z.B. (1971) The phosphorylation of yeast phosphoglycerate mutase. Arch. Biochem. Biophys., 146, 359-360.
    • (1971) Arch. Biochem. Biophys. , vol.146 , pp. 359-360
    • Rose, Z.B.1
  • 33
    • 0027201613 scopus 로고
    • Three-dimensional structure of rat acid phosphatase
    • Schneider, G., Lindqvist, Y. and Vihko, P. (1993) Three-dimensional structure of rat acid phosphatase. EMBO J., 12, 2609-2615.
    • (1993) EMBO J. , vol.12 , pp. 2609-2615
    • Schneider, G.1    Lindqvist, Y.2    Vihko, P.3
  • 34
    • 0018395990 scopus 로고
    • Purification and properties of phosphoglycerate phosphomutase from spores and cells of Bacillus megaterium
    • Singh, R.P. and Setlow, P. (1979) Purification and properties of phosphoglycerate phosphomutase from spores and cells of Bacillus megaterium. J. Bacteriol., 137, 1024-1027.
    • (1979) J. Bacteriol. , vol.137 , pp. 1024-1027
    • Singh, R.P.1    Setlow, P.2
  • 35
    • 0022477627 scopus 로고
    • Wheat germ phosphoglycerate mutase. Evidence for a metalloenzyme
    • Smith, G.C., McWilliams, A.D. and Hans, L.F. (1988) Wheat germ phosphoglycerate mutase. Evidence for a metalloenzyme. Biochem. Biophys. Res. Commun., 136, 336-340.
    • (1988) Biochem. Biophys. Res. Commun. , vol.136 , pp. 336-340
    • Smith, G.C.1    McWilliams, A.D.2    Hans, L.F.3
  • 36
    • 0028356059 scopus 로고
    • Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes
    • Sofia, H.J., Burland, V., Daniels, D.L., Plunkett, G., III and Blatter, F.R. (1994) Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes. Nucleic Acids Res., 22, 2576-2586.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2576-2586
    • Sofia, H.J.1    Burland, V.2    Daniels, D.L.3    Plunkett G. III4    Blatter, F.R.5
  • 38
    • 0032478539 scopus 로고    scopus 로고
    • Kinetic and X-ray structure studies of three mutant E.coli alkaline phosphatases: Insights into the catalytic mechanism without the nucleophile Ser102
    • Stec, B., Hehir, M.J., Brennan, C., Nolte, M. and Kantrowitz, E.R. (1998) Kinetic and X-ray structure studies of three mutant E.coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102. J. Mol. Biol., 277, 647-662.
    • (1998) J. Mol. Biol. , vol.277 , pp. 647-662
    • Stec, B.1    Hehir, M.J.2    Brennan, C.3    Nolte, M.4    Kantrowitz, E.R.5
  • 40
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T.C. and Berendzen, J. (1999) Automated MAD and MIR structure solution. Acta Crystallogr. D, 55, 849-861.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 41
    • 0018340984 scopus 로고
    • Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis
    • Watabe, K. and Freese, E. (1979) Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis. J. Bacteriol., 137, 773-778.
    • (1979) J. Bacteriol. , vol.137 , pp. 773-778
    • Watabe, K.1    Freese, E.2
  • 42
    • 0026752310 scopus 로고
    • Development of a mutagenesis, expression and purification system for yeast phosphoglycerate mutase
    • White, M.F. and Fothergill-Gilmore, L.A. (1992) Development of a mutagenesis, expression and purification system for yeast phosphoglycerate mutase. Eur. J. Biochem., 207, 709-714.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 709-714
    • White, M.F.1    Fothergill-Gilmore, L.A.2
  • 43
    • 0027322682 scopus 로고
    • Substitution of His-181 by alanine in yeast phosphoglycerate mutase leads to cofactor-induced dissociation of the tetrameric structure
    • White, M.F., Fothergill-Gilmore, L.A., Kelly, S.M. and Price, N.C. (1993) Substitution of His-181 by alanine in yeast phosphoglycerate mutase leads to cofactor-induced dissociation of the tetrameric structure. Biochem. J., 291, 479-483.
    • (1993) Biochem. J. , vol.291 , pp. 479-483
    • White, M.F.1    Fothergill-Gilmore, L.A.2    Kelly, S.M.3    Price, N.C.4


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