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Volumn 156, Issue 3, 2006, Pages 469-479

The three-dimensional structure of an eukaryotic glutamine synthetase: Functional implications of its oligomeric structure

Author keywords

Domain swapping; Electron microscopy; Glutamine synthetase; Oligomerization

Indexed keywords

ADENOSINE TRIPHOSPHATE; DIMER; ENZYME INHIBITOR; GLUTAMATE AMMONIA LIGASE; METHIONINE SULFOXIMINE; OLIGOMER; TETRAMER;

EID: 33751085376     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.06.003     Document Type: Article
Times cited : (54)

References (46)
  • 1
    • 0035834745 scopus 로고    scopus 로고
    • Structure prediction and active site analysis of the metal binding determinants in gamma-glutamylcysteine synthetase
    • Abbott J.J., Pei J., Ford J.L., Qi Y., Grishin V.N., Pitcher L.A., Phillips M.A., and Grishin N.V. Structure prediction and active site analysis of the metal binding determinants in gamma-glutamylcysteine synthetase. J. Biol. Chem. 276 (2001) 42099-42107
    • (2001) J. Biol. Chem. , vol.276 , pp. 42099-42107
    • Abbott, J.J.1    Pei, J.2    Ford, J.L.3    Qi, Y.4    Grishin, V.N.5    Pitcher, L.A.6    Phillips, M.A.7    Grishin, N.V.8
  • 2
    • 0022776515 scopus 로고
    • Novel subunitsubunit interactions in the structure of glutamine synthetase
    • Almassy R.J., Janson C.A., Hamlin R., Huong N.H., and Eisenberg D. Novel subunitsubunit interactions in the structure of glutamine synthetase. Nature 323 (1986) 304-309
    • (1986) Nature , vol.323 , pp. 304-309
    • Almassy, R.J.1    Janson, C.A.2    Hamlin, R.3    Huong, N.H.4    Eisenberg, D.5
  • 3
    • 0037137034 scopus 로고    scopus 로고
    • ATP binding to purified homopolymeric plant glutamine synthetase studied by isothermal titration calorimetry
    • Betti M., Márquez A.J., Yanes C., and Maestre A. ATP binding to purified homopolymeric plant glutamine synthetase studied by isothermal titration calorimetry. Thermochim. Acta 394 (2002) 63-71
    • (2002) Thermochim. Acta , vol.394 , pp. 63-71
    • Betti, M.1    Márquez, A.J.2    Yanes, C.3    Maestre, A.4
  • 4
    • 0036757430 scopus 로고    scopus 로고
    • Glutamine synthetase isolated from human brain: octameric structure and homology of partial primary structure with human liver glutamine synthetase
    • Boksha I.S., Schönfeld H.J., Langen H., Müller F., Tereshkina E.B., and Burbaeba G.S. Glutamine synthetase isolated from human brain: octameric structure and homology of partial primary structure with human liver glutamine synthetase. Biochemistry (Moscow) 67 (2002) 1012-1020
    • (2002) Biochemistry (Moscow) , vol.67 , pp. 1012-1020
    • Boksha, I.S.1    Schönfeld, H.J.2    Langen, H.3    Müller, F.4    Tereshkina, E.B.5    Burbaeba, G.S.6
  • 5
    • 0033198858 scopus 로고    scopus 로고
    • Functional importance of Asp56 from the α-polypeptide of Phaseolus vulgaris glutamine synthetase. An essential residue for transferase but not for biosynthetic enzyme activity
    • Clemente M.T., and Márquez A.J. Functional importance of Asp56 from the α-polypeptide of Phaseolus vulgaris glutamine synthetase. An essential residue for transferase but not for biosynthetic enzyme activity. Eur. J. Biochem. 264 (1999) 453-460
    • (1999) Eur. J. Biochem. , vol.264 , pp. 453-460
    • Clemente, M.T.1    Márquez, A.J.2
  • 6
    • 0021234028 scopus 로고
    • Association-dissociation of mammalian brain glutamine synthetase: effects of metal ions and other ligands
    • Denman R.B., and Wedler F.C. Association-dissociation of mammalian brain glutamine synthetase: effects of metal ions and other ligands. Arch. Biochem. Biophys. 232 (1984) 427-440
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 427-440
    • Denman, R.B.1    Wedler, F.C.2
  • 7
    • 0023482099 scopus 로고
    • Some evolutionary relationships of the primary biological catalysts glutamine synthetase and RuBisCo
    • Eisenberg D. Some evolutionary relationships of the primary biological catalysts glutamine synthetase and RuBisCo. Cold Spring Harbor Quant. Biol. 52 (1987) 483-490
    • (1987) Cold Spring Harbor Quant. Biol. , vol.52 , pp. 483-490
    • Eisenberg, D.1
  • 9
    • 0022428126 scopus 로고
    • Cysteine residues at the active site of glutamine synthetase from spinach leaves
    • Ericson M.C., and Brunn S.A. Cysteine residues at the active site of glutamine synthetase from spinach leaves. Biochim. Biophys. Res. Commun. 133 (1985) 527-531
    • (1985) Biochim. Biophys. Res. Commun. , vol.133 , pp. 527-531
    • Ericson, M.C.1    Brunn, S.A.2
  • 10
    • 0035916242 scopus 로고    scopus 로고
    • The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition
    • Gill H.S., and Eisenberg D. The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition. Biochemistry 40 (2001) 1903-1912
    • (2001) Biochemistry , vol.40 , pp. 1903-1912
    • Gill, H.S.1    Eisenberg, D.2
  • 11
    • 0037031287 scopus 로고    scopus 로고
    • Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation
    • Gill H.S., Pfluegl G.M.U., and Eisenberg D. Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation. Biochemistry 41 (2002) 9863-9872
    • (2002) Biochemistry , vol.41 , pp. 9863-9872
    • Gill, H.S.1    Pfluegl, G.M.U.2    Eisenberg, D.3
  • 12
    • 0031473847 scopus 로고    scopus 로고
    • SWISS_MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS_MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 13
    • 0001583742 scopus 로고
    • Glutamine synthetase in rice: a comparative study of the enzymes from root and leaves
    • Hirel B., and Gadal P. Glutamine synthetase in rice: a comparative study of the enzymes from root and leaves. Plant Physiol. 66 (1980) 619-623
    • (1980) Plant Physiol. , vol.66 , pp. 619-623
    • Hirel, B.1    Gadal, P.2
  • 15
    • 0000320777 scopus 로고
    • Molecular composition of glutamine synthetase of Sinapsis alba L
    • Höpfner M., Reifferscheid G., and Wild A. Molecular composition of glutamine synthetase of Sinapsis alba L. Z. Naturforsch. 43c (1988) 194-198
    • (1988) Z. Naturforsch. , vol.43 c , pp. 194-198
    • Höpfner, M.1    Reifferscheid, G.2    Wild, A.3
  • 16
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones D.T. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292 (1999) 195-202
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 17
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 18
    • 85035288824 scopus 로고    scopus 로고
    • Kiang, C.-H., 2001. Single-particle study of protein assembly. Phys. Rev. E 64, 041911 1-3.
  • 19
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding S.E., Rowe A.J., and Horton J.C. (Eds), The Royal Society of Chemistry Cambridge
    • Laue T.M., Shall B.D., Ridgeway T.M., and Pelletier S.L. Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding S.E., Rowe A.J., and Horton J.C. (Eds). Analytical ultracentrifugation in biochemistry and polymer science (1992), The Royal Society of Chemistry Cambridge 90-125
    • (1992) Analytical ultracentrifugation in biochemistry and polymer science , pp. 90-125
    • Laue, T.M.1    Shall, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 20
    • 3042842012 scopus 로고    scopus 로고
    • YbdK is a carboxylate-amine ligase with a gamma-glutamyl:cysteine ligase activity: crystal structure and enzymatic assays
    • Lehmann C., Doseeva V., Pullalarevu S., Krajewski W., Howard A., and Herzberg O. YbdK is a carboxylate-amine ligase with a gamma-glutamyl:cysteine ligase activity: crystal structure and enzymatic assays. Proteins 56 (2004) 376-383
    • (2004) Proteins , vol.56 , pp. 376-383
    • Lehmann, C.1    Doseeva, V.2    Pullalarevu, S.3    Krajewski, W.4    Howard, A.5    Herzberg, O.6
  • 21
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: as domains continue to swap
    • Liu Y., and Eisenberg D. 3D domain swapping: as domains continue to swap. Protein Sci. 11 (2002) 1285-1299
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 22
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semi automated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semi automated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 23
    • 0032068626 scopus 로고    scopus 로고
    • Glutamine synthetase isoenzymes, oligomers and subunits from hairy roots of Beta vulgaris L. var. lutea
    • Mäck G. Glutamine synthetase isoenzymes, oligomers and subunits from hairy roots of Beta vulgaris L. var. lutea. Planta 205 (1998) 113-120
    • (1998) Planta , vol.205 , pp. 113-120
    • Mäck, G.1
  • 24
    • 0022332813 scopus 로고
    • Active-site ligand binding and subunit interactions in glutamine synthetase from Escherichia coli
    • Maurizi M.R., and Ginsburg A. Active-site ligand binding and subunit interactions in glutamine synthetase from Escherichia coli. Curr. Top. Cell. Reg. 26 (1985) 191-206
    • (1985) Curr. Top. Cell. Reg. , vol.26 , pp. 191-206
    • Maurizi, M.R.1    Ginsburg, A.2
  • 25
    • 0022559036 scopus 로고
    • Mg2+ is bound to glutamine synthetase extracted from bovine or ovine in the presence of l-methionine-S-sulphoximine phosphate
    • Maurizi M.R., Pinfofsky H.B., McFarland P.J., and Ginsburg A. Mg2+ is bound to glutamine synthetase extracted from bovine or ovine in the presence of l-methionine-S-sulphoximine phosphate. Arch. Biohem. Biophys. 256 (1986) 494-500
    • (1986) Arch. Biohem. Biophys. , vol.256 , pp. 494-500
    • Maurizi, M.R.1    Pinfofsky, H.B.2    McFarland, P.J.3    Ginsburg, A.4
  • 26
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L.J., Bryson K., and Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 16 (2000) 404-405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 27
    • 0017229851 scopus 로고
    • The purification and properties of the glutamine synthetase from the cytosol of soya-bean root nodules
    • McParland R.H., Guevara J.G., Becker R.R., and Evans H.J. The purification and properties of the glutamine synthetase from the cytosol of soya-bean root nodules. Biochem. J. 153 (1976) 597-606
    • (1976) Biochem. J. , vol.153 , pp. 597-606
    • McParland, R.H.1    Guevara, J.G.2    Becker, R.R.3    Evans, H.J.4
  • 28
    • 0041344552 scopus 로고    scopus 로고
    • Distinctive properties and expression profiles of glutamine synthetase from a plant symbiotic fungus
    • Montanini B., Betti M., Márquez A.J., Balestrini R., Bonfante P., and Ottonello S. Distinctive properties and expression profiles of glutamine synthetase from a plant symbiotic fungus. Biochem. J. 373 (2003) 357-368
    • (2003) Biochem. J. , vol.373 , pp. 357-368
    • Montanini, B.1    Betti, M.2    Márquez, A.J.3    Balestrini, R.4    Bonfante, P.5    Ottonello, S.6
  • 30
    • 0028961335 scopus 로고
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures
    • Murzin A.G., Brenner S.E., Hubbard T., and Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247 (1995) 536-540
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 31
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: a novel method for fast and accurate multiple sequence alignment
    • Notredame C., Higgins D.G., and Heringa J. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302 (2000) 205-217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 32
    • 0031036440 scopus 로고    scopus 로고
    • An improved function for fitting sedimentation velocity data for low molecular-weight solutes
    • Philo J.S. An improved function for fitting sedimentation velocity data for low molecular-weight solutes. Biophys. J. 72 (1997) 435-444
    • (1997) Biophys. J. , vol.72 , pp. 435-444
    • Philo, J.S.1
  • 35
    • 0014483560 scopus 로고
    • Studies on the mechanism of inhibition of glutamine synthetase by methionine sulfoximine
    • Ronzio R.A., Rowe W.B., and Meister A. Studies on the mechanism of inhibition of glutamine synthetase by methionine sulfoximine. Biochemistry 8 (1969) 1066-1075
    • (1969) Biochemistry , vol.8 , pp. 1066-1075
    • Ronzio, R.A.1    Rowe, W.B.2    Meister, A.3
  • 36
    • 0029862804 scopus 로고    scopus 로고
    • Molecular identification and characterization of cytosolic isoforms of glutamine synthetase in maize roots
    • Sakakibara H., Shimizu H., Hase T., Yamazaki Y., Takao T., Shimonishi Y., and Sugiyama T. Molecular identification and characterization of cytosolic isoforms of glutamine synthetase in maize roots. J. Biol. Chem. 271 (1996) 29561-29568
    • (1996) J. Biol. Chem. , vol.271 , pp. 29561-29568
    • Sakakibara, H.1    Shimizu, H.2    Hase, T.3    Yamazaki, Y.4    Takao, T.5    Shimonishi, Y.6    Sugiyama, T.7
  • 37
    • 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
  • 38
    • 0014007813 scopus 로고
    • Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulphite and hydroxylamine reductases
    • Siegel L.M., and Monty K.J. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulphite and hydroxylamine reductases. Biochim. Biophys. Acta 112 (1966) 346-362
    • (1966) Biochim. Biophys. Acta , vol.112 , pp. 346-362
    • Siegel, L.M.1    Monty, K.J.2
  • 39
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl M.J. Recognition of errors in three-dimensional structures of proteins. Proteins 17 (1993) 355-362
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 40
    • 77956892020 scopus 로고
    • The glutamine synthetase of Escherichia coli: structure and control
    • Boyer P.D. (Ed), Academic Press, New York
    • Stadtman E.R., and Ginsburg A. The glutamine synthetase of Escherichia coli: structure and control. In: Boyer P.D. (Ed). The Enzymes vol. 10 (1974), Academic Press, New York 755-807
    • (1974) The Enzymes , vol.10 , pp. 755-807
    • Stadtman, E.R.1    Ginsburg, A.2
  • 41
    • 0033780375 scopus 로고    scopus 로고
    • Prediction of protein interactions: metabolic enzymes are frequently involved in gene fusion
    • Tsoka S., and Ouzounis C.A. Prediction of protein interactions: metabolic enzymes are frequently involved in gene fusion. Nat. Genet. 26 (2000) 141-142
    • (2000) Nat. Genet. , vol.26 , pp. 141-142
    • Tsoka, S.1    Ouzounis, C.A.2
  • 43
    • 0015041887 scopus 로고
    • Regulation of rat liver glutamine synthetases: activation by α-ketoglutarate and inhibition by glycine, alanine and carbamyl phosphate
    • Tate S.S., and Meister A. Regulation of rat liver glutamine synthetases: activation by α-ketoglutarate and inhibition by glycine, alanine and carbamyl phosphate. Proc. Natl. Acad. Sci. USA 68 (1971) 781-785
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 781-785
    • Tate, S.S.1    Meister, A.2
  • 44
    • 0015501672 scopus 로고
    • Rat liver glutamine synthetase. Preparation, properties and mechanism of inhibition by carbamyl phosphate
    • Tate S.S., Leu F.Y., and Meister A. Rat liver glutamine synthetase. Preparation, properties and mechanism of inhibition by carbamyl phosphate. J. Biol. Chem. 247 (1972) 5312-5321
    • (1972) J. Biol. Chem. , vol.247 , pp. 5312-5321
    • Tate, S.S.1    Leu, F.Y.2    Meister, A.3
  • 46
    • 0020477024 scopus 로고
    • Glutamine synthetase from ovine brain is a manganese (II) enzyme
    • Wedler F.C., Denman R.B., and Roby W.G. Glutamine synthetase from ovine brain is a manganese (II) enzyme. Biochemistry 21 (1982) 6389-6396
    • (1982) Biochemistry , vol.21 , pp. 6389-6396
    • Wedler, F.C.1    Denman, R.B.2    Roby, W.G.3


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