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Volumn 266, Issue 4, 1997, Pages 847-856

The role of the metal ion in the p21(ras) catalysed GTP-hydrolysis: Mn2+ versus Mg2+

Author keywords

3D structure; GTP hydrolysis; Manganese; Metal ion; Ras p21

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; GUANOSINE TRIPHOSPHATE; MAGNESIUM ION; MANGANESE; METAL ION; PHOSPHATE; RAS PROTEIN;

EID: 0031557398     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0814     Document Type: Article
Times cited : (53)

References (61)
  • 2
    • 0028105959 scopus 로고
    • Structural studies of metal binding by inositol monophosphatase: Evidence for two-metal ion catalysis
    • Bone R., Frank L., Springer J. P., Atack J. R. Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis. Biochemistry. 33:1994;9468-9467.
    • (1994) Biochemistry , vol.33 , pp. 9468-9467
    • Bone, R.1    Frank, L.2    Springer, J.P.3    Atack, J.R.4
  • 4
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne H. R., Sanders D. A., McCormick F. The GTPase superfamily: a conserved switch for diverse cell functions. Nature. 348:1990;125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0018287755 scopus 로고
    • A study of the mechanism of DNA polymerase I from Escherichia coli with diastereomeric phosphorothioate analogs of deoxyadenosine triphosphate
    • Burgers P. M. J., Eckstein F. A study of the mechanism of DNA polymerase I from Escherichia coli with diastereomeric phosphorothioate analogs of deoxyadenosine triphosphate. J. Biol. Chem. 254:1979;6889-6893.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6889-6893
    • Burgers, P.M.J.1    Eckstein, F.2
  • 9
    • 0001859381 scopus 로고
    • The Role of Divalent Metal Ions in Phosphoryl and Nucleotidyl Transfer
    • New York and Basel: Marcel Dekker, Inc.
    • Cooperman B. S. The Role of Divalent Metal Ions in Phosphoryl and Nucleotidyl Transfer. Metal Ions in Biological Systems. 1976;Marcel Dekker, Inc. New York and Basel.
    • (1976) Metal Ions in Biological Systems
    • Cooperman, B.S.1
  • 10
    • 0019879371 scopus 로고
    • Divalent metal ion, inorganic phosphate, and inorganic phosphate analogue binding to yeast inorganic pyrophospatase
    • Cooperman B. S., Panackal A., Springs B., Hamm D. J. Divalent metal ion, inorganic phosphate, and inorganic phosphate analogue binding to yeast inorganic pyrophospatase. Biochemistry. 20:1981;6051-6060.
    • (1981) Biochemistry , vol.20 , pp. 6051-6060
    • Cooperman, B.S.1    Panackal, A.2    Springs, B.3    Hamm, D.J.4
  • 12
    • 0028902882 scopus 로고
    • Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL
    • Diamant S., Azem A., Weiss C., Goloubinoff P. Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL. Biochemistry. 34:1995;273-277.
    • (1995) Biochemistry , vol.34 , pp. 273-277
    • Diamant, S.1    Azem, A.2    Weiss, C.3    Goloubinoff, P.4
  • 13
    • 0025944583 scopus 로고
    • Experimental designs for estimating the parameters of the Michaelis-Menten equation from progress curves of enzyme-catalyzed reactions
    • Duggleby R. G., Clarke R. B. Experimental designs for estimating the parameters of the Michaelis-Menten equation from progress curves of enzyme-catalyzed reactions. Biochim. Biophys. Acta. 1080:1991;231-236.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 231-236
    • Duggleby, R.G.1    Clarke, R.B.2
  • 15
    • 0026512963 scopus 로고
    • Metal activation of synthetic and degradative activites of θ29 DNA polymerase, a model enzyme for protein-primed DNA replication
    • Esteban J. A., Bernad A., Salas M., Blanco L. Metal activation of synthetic and degradative activites of θ29 DNA polymerase, a model enzyme for protein-primed DNA replication. Biochemistry. 31:1992;350-359.
    • (1992) Biochemistry , vol.31 , pp. 350-359
    • Esteban, J.A.1    Bernad, A.2    Salas, M.3    Blanco, L.4
  • 18
    • 0026711081 scopus 로고
    • Mutational and kinetic analysis of the GTPase-activating protein (GAP)-p21 interaction: The C-terminal domain of GAP is not sufficient for full activity
    • Gideon P., John J., Frech M., Lautwein A., Clark R., Scheffler J. E., Wittinghofer A. Mutational and kinetic analysis of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity. Mol. Cell. Biol. 12:1992;2050-2056.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2050-2056
    • Gideon, P.1    John, J.2    Frech, M.3    Lautwein, A.4    Clark, R.5    Scheffler, J.E.6    Wittinghofer, A.7
  • 19
    • 0019887609 scopus 로고
    • Modulation by monovalent and divalent cations of the guanosine-5′-triphosphatase activiy dependent on elongation factor Tu
    • Ivell R., Sander G., Parmeggiani A. Modulation by monovalent and divalent cations of the guanosine-5′-triphosphatase activiy dependent on elongation factor Tu. Biochemistry. 20:1981;6852-6859.
    • (1981) Biochemistry , vol.20 , pp. 6852-6859
    • Ivell, R.1    Sander, G.2    Parmeggiani, A.3
  • 22
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones T. A. A graphics model building and refinement system for macromolecules. J. Appl. Crystallog. 11:1978;268-272.
    • (1978) J. Appl. Crystallog. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 23
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26:1993;795-800.
    • (1993) J. Appl. Crystallog , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 24
    • 0011387138 scopus 로고
    • Identification of oxygen ligands in metal-nucleotide-protein complexes by observation of the Mn(II)-17O superhyperfine coupling
    • H. Sigel. New York and Basel: Marcel Dekker, Inc.
    • Kalbitzer H. R. Identification of oxygen ligands in metal-nucleotide-protein complexes by observation of the Mn(II)-17O superhyperfine coupling. Sigel H. Metal Ions in Biological Systems. 1987;Marcel Dekker, Inc. New York and Basel.
    • (1987) Metal Ions in Biological Systems
    • Kalbitzer, H.R.1
  • 25
    • 0026666130 scopus 로고
    • A trinucleotide can promote metal ion-dependent specific cleavage of RNA
    • Kazakov S., Altmann S. A trinucleotide can promote metal ion-dependent specific cleavage of RNA. Proc. Natl Acad. Sci. USA. 89:1992;7939-7934.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 7939-7934
    • Kazakov, S.1    Altmann, S.2
  • 26
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • Kjeldgaard M., Nissen P., Thirup S., Nyborg J. The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure. 1:1993;35-50.
    • (1993) Structure , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3    Nyborg, J.4
  • 28
    • 0028204451 scopus 로고
    • Solution structure and dynamics of Ras p21·GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy
    • Kraulis P. J., Domaille P. J., Campbell-Burk S. L., Van Aken T., Laue E. D. Solution structure and dynamics of Ras p21·GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry. 33:1994;3515-3531.
    • (1994) Biochemistry , vol.33 , pp. 3515-3531
    • Kraulis, P.J.1    Domaille, P.J.2    Campbell-Burk, S.L.3    Van Aken, T.4    Laue, E.D.5
  • 29
    • 0025193871 scopus 로고
    • Three-dimensional structures of H-ras p21 mutants: Molecular basis for their inability to function as signal switch molecules
    • Krengel U., Schlichting I., Scherer A., Schumann R., Frech M., John J., Kabsch W., Pai E. F., Wittinghofer A. Three-dimensional structures of H-ras p21 mutants: molecular basis for their inability to function as signal switch molecules. Cell. 62:1990;539-548.
    • (1990) Cell , vol.62 , pp. 539-548
    • Krengel, U.1    Schlichting, I.2    Scherer, A.3    Schumann, R.4    Frech, M.5    John, J.6    Kabsch, W.7    Pai, E.F.8    Wittinghofer, A.9
  • 31
    • 0021104956 scopus 로고
    • Stereochemistry of the elongation factor Tu-GTP complex
    • Leupold C. M., Goody R. S., Wittinghofer A. Stereochemistry of the elongation factor Tu-GTP complex. Eur. J. Biochem. 135:1983;237-241.
    • (1983) Eur. J. Biochem. , vol.135 , pp. 237-241
    • Leupold, C.M.1    Goody, R.S.2    Wittinghofer, A.3
  • 33
    • 0001099937 scopus 로고
    • Traitements statistique des erreurs dans la détermination des structures cristallines
    • Luzzati P. V. Traitements statistique des erreurs dans la détermination des structures cristallines. Acta Crystallog. 5:1952;802-810.
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, P.V.1
  • 34
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenicras proteins
    • Milburn M. V., Tong L., DeVos A. M., Brünger A., Yamaizumi Z., Nishimura S., Kim S.-H. Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenicras proteins. Science. 247:1990;939-945.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    DeVos, A.M.3    Brünger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.-H.7
  • 36
    • 0028305912 scopus 로고
    • A G protein involved in nucleocytoplasmic transport: The role of Ran
    • Moore M. S., Blobel G. A G protein involved in nucleocytoplasmic transport: the role of Ran. Trends Biochem. Sci. 19:1994;211-216.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 211-216
    • Moore, M.S.1    Blobel, G.2
  • 37
    • 0029107760 scopus 로고
    • The 2.2. Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf-1 in complex with Rap1A and a GTP analogue
    • Nassar N., Horn G., Herrmann C., Scherer A., McCormick F., Wittinghofer A. The 2.2. Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf-1 in complex with Rap1A and a GTP analogue. Nature. 375:1995;554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 38
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducin-γ complexed with GTPγS
    • Noel J. P., Hamm H. E., Sigler P. B. The 2.2 Å crystal structure of transducin-γ complexed with GTPγS. Nature. 366:1993;654-663.
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 39
    • 0024463212 scopus 로고
    • Structure of the guanine-nucleotide-binding domain of the Ha- ras oncogene product p21 in the triphosphate conformation
    • Pai E. F., Kabsch W., Krengel U., Holmes K. C., John J., Wittinghofer A. Structure of the guanine-nucleotide-binding domain of the Ha- ras oncogene product p21 in the triphosphate conformation. Nature. 341:1989;209-214.
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.F.1    Kabsch, W.2    Krengel, U.3    Holmes, K.C.4    John, J.5    Wittinghofer, A.6
  • 40
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: Implications for the mechanism of GTP hydrolysis
    • Pai E. F., Krengel U., Petsko G. A., Goody R. S., Kabsch W., Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9:1990;2351-2359.
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 41
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read R. J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect A. 42:1986;140-149.
    • (1986) Acta Crystallog. Sect A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 42
    • 0026002058 scopus 로고
    • P21 with a Phe_Leu mutation interacts normally with GTPase activating protein GAP but is nevertheless transforming
    • Reinstein J., Schlichting I., Frech M., Goody R. S., Wittinghofer A. p21 with a Phe_Leu mutation interacts normally with GTPase activating protein GAP but is nevertheless transforming. J. Biol. Chem. 266:1991;17700-17706.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17700-17706
    • Reinstein, J.1    Schlichting, I.2    Frech, M.3    Goody, R.S.4    Wittinghofer, A.5
  • 43
    • 0026349335 scopus 로고
    • Is there a rate limiting step before GTP cleavage by H-ras p21?
    • Rensland H., Lautwein A., Wittinghofer A., Goody R. S. Is there a rate limiting step before GTP cleavage by H-ras p21? Biochemistry. 30:1991;11181-11185.
    • (1991) Biochemistry , vol.30 , pp. 11181-11185
    • Rensland, H.1    Lautwein, A.2    Wittinghofer, A.3    Goody, R.S.4
  • 44
    • 0028136070 scopus 로고
    • Crystal structure of rat DNA polymerase β: Evidence for a common polymerase mechanism
    • Sawaya M. R., Pelletier H., Kumar A., Wilson S. H., Kraut J. Crystal structure of rat DNA polymerase β: evidence for a common polymerase mechanism. Science. 264:1994;1930-1935.
    • (1994) Science , vol.264 , pp. 1930-1935
    • Sawaya, M.R.1    Pelletier, H.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 45
    • 0024511374 scopus 로고
    • Crystallization and preliminary X-ray analysis of the human c-H-ras oncogene product p21 complexed with GTP analogues
    • Scherer A., John J., Linke R., Goody R. S., Wittinghofer A., Pai E. F., Holmes K. C. Crystallization and preliminary X-ray analysis of the human c-H-ras oncogene product p21 complexed with GTP analogues. J. Mol. Biol. 206:1989;257-259.
    • (1989) J. Mol. Biol. , vol.206 , pp. 257-259
    • Scherer, A.1    John, J.2    Linke, R.3    Goody, R.S.4    Wittinghofer, A.5    Pai, E.F.6    Holmes, K.C.7
  • 46
    • 0028448284 scopus 로고
    • Structures, interactions and relationships
    • Schweins T., Wittinghofer A. Structures, interactions and relationships. Curr. Biol. 4:1994;547-550.
    • (1994) Curr. Biol. , vol.4 , pp. 547-550
    • Schweins, T.1    Wittinghofer, A.2
  • 47
    • 0028464366 scopus 로고
    • Why have mutagenesis studies not located the general base in ras p21?
    • Schweins T., Langen R., Warshel A. Why have mutagenesis studies not located the general base in ras p21? Struct. Biol. 1:1994;476-484.
    • (1994) Struct. Biol. , vol.1 , pp. 476-484
    • Schweins, T.1    Langen, R.2    Warshel, A.3
  • 49
    • 0029825324 scopus 로고    scopus 로고
    • Linear free energy relationships in the intrinsic and GAP-stimulated GTP-hydrolysis reaction
    • Schweins T., Geyer M., Kalbitzer H. R., Wittinghofer A., Warshel A. Linear free energy relationships in the intrinsic and GAP-stimulated GTP-hydrolysis reaction. Biochemistry. 35:1996;14225-14231.
    • (1996) Biochemistry , vol.35 , pp. 14225-14231
    • Schweins, T.1    Geyer, M.2    Kalbitzer, H.R.3    Wittinghofer, A.4    Warshel, A.5
  • 50
    • 0025300837 scopus 로고
    • Electron paramagnetic resonance measurements of the hydration of Mn(II) in ternary complexes with GDP and ras p21 proteins
    • Smithers G. W., Poe M., Latwesen D. G., Reed G. H. Electron paramagnetic resonance measurements of the hydration of Mn(II) in ternary complexes with GDP and ras p21 proteins. Arch. Biochem. Biophys. 280:1990;416-420.
    • (1990) Arch. Biochem. Biophys. , vol.280 , pp. 416-420
    • Smithers, G.W.1    Poe, M.2    Latwesen, D.G.3    Reed, G.H.4
  • 52
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for cytalytic RNA
    • Steitz T. A., Steitz J. A. A general two-metal-ion mechanism for cytalytic RNA. Proc. Natl Acad. Sci. USA. 90:1993;6498-6502.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 53
    • 0028606031 scopus 로고
    • A unified polymerase mechanism for nonhomologous DNA and RNA polymerases
    • Steitz T. A., Smerdon S. J., Jäger J., Joyce C. M. A unified polymerase mechanism for nonhomologous DNA and RNA polymerases. Science. 266:1994;2022-2025.
    • (1994) Science , vol.266 , pp. 2022-2025
    • Steitz, T.A.1    Smerdon, S.J.2    Jäger, J.3    Joyce, C.M.4
  • 54
    • 0026500416 scopus 로고
    • The structure of the E.coli recA protein monomer and polymer
    • Story M. R., Weber I. T., Steitz T. A. The structure of the E.coli recA protein monomer and polymer. Nature. 355:1992;318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, M.R.1    Weber, I.T.2    Steitz, T.A.3
  • 56
    • 0026086679 scopus 로고
    • Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogene mutant complexed with GDP
    • Tong L., deVos A. M., Milburn M. V., Kim S.-H. Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogene mutant complexed with GDP. J. Mol. Biol. 217:1991;503-516.
    • (1991) J. Mol. Biol. , vol.217 , pp. 503-516
    • Tong, L.1    DeVos, A.M.2    Milburn, M.V.3    Kim, S.-H.4
  • 57
    • 0022727887 scopus 로고
    • Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide-binding site
    • Tucker J., Sczakiel G., Feuerstein J., John J., Goody R. S., Wittinghofer A. Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide-binding site. EMBO J. 5:1986;1351-1358.
    • (1986) EMBO J. , vol.5 , pp. 1351-1358
    • Tucker, J.1    Sczakiel, G.2    Feuerstein, J.3    John, J.4    Goody, R.S.5    Wittinghofer, A.6
  • 58
    • 0026628624 scopus 로고
    • Eco RV restriction endonuclease: Communication between catalytic metal ions and DNA recognition
    • Vermote C. L., Halford S. E. Eco RV restriction endonuclease: communication between catalytic metal ions and DNA recognition. Biochemistry. 31:1992;6082-6089.
    • (1992) Biochemistry , vol.31 , pp. 6082-6089
    • Vermote, C.L.1    Halford, S.E.2
  • 59
    • 0026755152 scopus 로고
    • Eco RV restriction endonuclease: Communication between DNA recognition and catalysis
    • Vermote C. L., Vipond I. B., Halford S. E. Eco RV restriction endonuclease: communication between DNA recognition and catalysis. Biochemistry. 31:1992;6089-6097.
    • (1992) Biochemistry , vol.31 , pp. 6089-6097
    • Vermote, C.L.1    Vipond, I.B.2    Halford, S.E.3
  • 60
    • 0018330836 scopus 로고
    • 2+on some properties of nucleotide-free elongation factor Tu from Bacillus stearothermophilus
    • 2+on some properties of nucleotide-free elongation factor Tu from Bacillus stearothermophilus. Eur. J. Biochem. 93:1979;95-101.
    • (1979) Eur. J. Biochem. , vol.93 , pp. 95-101
    • Wittinghofer, A.1    Leberman, R.2
  • 61
    • 0000127673 scopus 로고
    • 2.2 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor
    • Zheng J., Trafny E. A., Knighton D. R., Xuong N.-H., Taylor S. S., Ten Eyck L. F., Sowadski J. M. 2.2 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor. Acta Crystallog. sect. D. 49:1993;362-365.
    • (1993) Acta Crystallog. Sect. D , vol.49 , pp. 362-365
    • Zheng, J.1    Trafny, E.A.2    Knighton, D.R.3    Xuong, N.-H.4    Taylor, S.S.5    Ten Eyck, L.F.6    Sowadski, J.M.7


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