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Volumn 43, Issue 2, 2004, Pages 352-361

Parallel Evolutionary Pathways for Glutathione Transferases: Structure and Mechanism of the Mitochondrial Class Kappa Enzyme rGSTK1-1

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; ESCHERICHIA COLI; HYDROGEN BONDS; IONIZATION; PROTEINS; SULFUR;

EID: 0345832239     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035832z     Document Type: Article
Times cited : (118)

References (38)
  • 1
    • 0031021397 scopus 로고    scopus 로고
    • Catalytic mechanism and evolution of the glutathione transferases
    • Armstrong, R. N. (1997) Catalytic mechanism and evolution of the glutathione transferases, Chem. Res. Toxicol. 10, 2-18.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 2
    • 0033011878 scopus 로고    scopus 로고
    • Common structural features of MAPEG-A widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism
    • Jakobsson, P.-J., Morgenstern, R., Mancini, J., Ford-Hutchinson, A., and Persson, B. (1999) Common structural features of MAPEG-A widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism, Protein Sci. 8, 689-692.
    • (1999) Protein Sci. , vol.8 , pp. 689-692
    • Jakobsson, P.-J.1    Morgenstern, R.2    Mancini, J.3    Ford-Hutchinson, A.4    Persson, B.5
  • 3
    • 0034649338 scopus 로고    scopus 로고
    • Mechanistic diversity in a metalloenzyme superfamily
    • Armstrong, R. N. (2000) Mechanistic diversity in a metalloenzyme superfamily, Biochemistry 39, 13625-13632.
    • (2000) Biochemistry , vol.39 , pp. 13625-13632
    • Armstrong, R.N.1
  • 4
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: Implications for classification of nonmammalian Members of an ancient enzyme superfamily
    • Sheehan, D., Meade, G., Foley, V. M., and Dowd, C. A. (2001) Structure, function and evolution of glutathione transferases: Implications for classification of nonmammalian Members of an ancient enzyme superfamily, Biochem. J. 360, 1-16.
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 6
    • 0037018936 scopus 로고    scopus 로고
    • Structure of a tau class glutathione S-transferase from wheat active in herbicide detoxification
    • Thom, R., Cummins, I., Dixon, D. P., Edwards, R., Cole, D. J., and Lapthorn, A. J. (2002) Structure of a tau class glutathione S-transferase from wheat active in herbicide detoxification, Biochemistry 41, 7008-7020.
    • (2002) Biochemistry , vol.41 , pp. 7008-7020
    • Thom, R.1    Cummins, I.2    Dixon, D.P.3    Edwards, R.4    Cole, D.J.5    Lapthorn, A.J.6
  • 7
    • 0018878263 scopus 로고
    • Resolution, purification and some properties of three glutathione transferases from rat liver mitochondria
    • Kraus, P. (1980) Resolution, purification and some properties of three glutathione transferases from rat liver mitochondria, Hoppe-Seyler's Z. Physiol. Chem. 361, 9-15.
    • (1980) Hoppe-Seyler's Z. Physiol. Chem. , vol.361 , pp. 9-15
    • Kraus, P.1
  • 8
    • 0025916806 scopus 로고
    • A novel glutathione transferase (13-13) isolated from the matrix of rat liver mitochondria having structural similarity to class theta enzymes
    • Harris, J. M., Meyer, D. J., Coles, B., and Ketterer, B. (1991) A novel glutathione transferase (13-13) isolated from the matrix of rat liver mitochondria having structural similarity to class theta enzymes, Biochem. J. 278, 137-141.
    • (1991) Biochem. J. , vol.278 , pp. 137-141
    • Harris, J.M.1    Meyer, D.J.2    Coles, B.3    Ketterer, B.4
  • 9
    • 0029854518 scopus 로고    scopus 로고
    • Glutathione S-transferase class kappa: Characterization by the cloning of rat mitochondrial GST and identification of a human homologue
    • Pemble, S. E., Wardle, A. F., and Taylor, J. B. (1996) Glutathione S-transferase class kappa: Characterization by the cloning of rat mitochondrial GST and identification of a human homologue, Biochem. J. 319, 749-754.
    • (1996) Biochem. J. , vol.319 , pp. 749-754
    • Pemble, S.E.1    Wardle, A.F.2    Taylor, J.B.3
  • 10
    • 0041845184 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of a murine class kappa glutathione S-transferase
    • Jowsey, I. R., Thomson, R. E., Orton, T. C., Elcombe, C. R., and Hayes, J. D. (2003) Biochemical and genetic characterization of a murine class kappa glutathione S-transferase, Biochem. J. 373, 559-569.
    • (2003) Biochem. J. , vol.373 , pp. 559-569
    • Jowsey, I.R.1    Thomson, R.E.2    Orton, T.C.3    Elcombe, C.R.4    Hayes, J.D.5
  • 12
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin, J. L., Bardwell, J. C., and Kuriyan, J. (1993) Crystal structure of the DsbA protein required for disulphide bond formation in vivo, Nature 365, 464-468.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.2    Kuriyan, J.3
  • 13
    • 0027937786 scopus 로고
    • Organization and evolution of naphthalene catabolic pathways: Sequence of the DNA encoding 2-hydroxychromene-2-carboxylate isomerase and trans-o-hydroxybenzyl-idenepyruvate hydratase-aldolase from the NAH7 plasmid
    • Eaton, R. W. (1994) Organization and evolution of naphthalene catabolic pathways: sequence of the DNA encoding 2-hydroxychromene-2-carboxylate isomerase and trans-o-hydroxybenzyl-idenepyruvate hydratase-aldolase from the NAH7 plasmid, J. Bacteriol. 176, 7757-7762.
    • (1994) J. Bacteriol. , vol.176 , pp. 7757-7762
    • Eaton, R.W.1
  • 14
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath, J. W. (1999) The finer things in X-ray diffraction data collection, Acta Crystallogr. D55, 1718-1725.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 15
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1996) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 277, 307-326.
    • (1996) Methods Enzymol. , vol.277 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 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. D55, 849-861.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 17
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • Terwilliger, T. C. (2002) Automated structure solution, density modification and model building, Acta Crystallogr. D58, 1937-1940.
    • (2002) Acta Crystallogr. , vol.D58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 18
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of Macromolecular Structures by the Maximum-Likelihood Method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallogr. D53, 240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 20
    • 0346743567 scopus 로고    scopus 로고
    • Practical Protein Crystallography, 2nd ed., Academic Press, San Diego
    • McRee, D. E. (1999) Practical Protein Crystallography, 2nd ed., Academic Press, San Diego.
    • (1999)
    • McRee, D.E.1
  • 21
    • 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. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 22
    • 0026705291 scopus 로고
    • Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase
    • Liu, S., Zhang, P., Ji, X., Johnson, W. W., Gilliland, G. L., and Armstrong, R. N. (1992) Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase, J. Biol. Chem. 267, 4296-4299.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4296-4299
    • Liu, S.1    Zhang, P.2    Ji, X.3    Johnson, W.W.4    Gilliland, G.L.5    Armstrong, R.N.6
  • 23
    • 0032485881 scopus 로고    scopus 로고
    • Enzymes Harboring Unnatural Amino Acids. Mechanistic and structural analysis of the enhanced catalytic activity of a glutathione transferase containing 5-fluorotryptophan
    • Parsons, J. F., Xiao, G., Gilliland, G. L., and Armstrong, R. N. (1998) Enzymes Harboring Unnatural Amino Acids. Mechanistic and structural analysis of the enhanced catalytic activity of a glutathione transferase containing 5-fluorotryptophan, Biochemistry 37, 6286-6294.
    • (1998) Biochemistry , vol.37 , pp. 6286-6294
    • Parsons, J.F.1    Xiao, G.2    Gilliland, G.L.3    Armstrong, R.N.4
  • 24
    • 0024588467 scopus 로고
    • Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase
    • Graminski, G. F., Kubo, Y., and Armstrong, R. N. (1989) Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase, Biochemistry 28, 3562-3568.
    • (1989) Biochemistry , vol.28 , pp. 3562-3568
    • Graminski, G.F.1    Kubo, Y.2    Armstrong, R.N.3
  • 25
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrixes
    • Holm, L., and Sander, C. (1993) Protein structure comparison by alignment of distance matrixes, J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 26
    • 0347373917 scopus 로고    scopus 로고
    • DeLano, W. L. PYMOL (The PyMOL Molecular Graphics System [http://www.pymol.org]).
    • DeLano, W.L.1
  • 27
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson, E. G., and Thornton, J. M. (1996) PROMOTIF- -a program to identify and analyze structural motifs in proteins, Protein Sci. 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 28
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon, D. J., and Anderson, W. F. (1988) A fast algorithm for rendering space-filling molecule pictures, J. Mol. Graphics 6, 219-220.
    • (1988) J. Mol. Graphics , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.F.2
  • 29
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A., and Bacon, D. J. (1997) Raster3D: Photorealistic molecular graphics, Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 30
    • 0035916913 scopus 로고    scopus 로고
    • Kinetic Analysis of the Slow Ionization of Glutathione by Microsomal Glutathione Transferase MGST1
    • Morgenstern, R., Svensson, R., Bernat, B. A., and Armstrong, R. N. (2001) Kinetic Analysis of the Slow Ionization of Glutathione by Microsomal Glutathione Transferase MGST1, Biochemistry 40, 3378-3384.
    • (2001) Biochemistry , vol.40 , pp. 3378-3384
    • Morgenstern, R.1    Svensson, R.2    Bernat, B.A.3    Armstrong, R.N.4
  • 31
    • 0347997288 scopus 로고    scopus 로고
    • Local protein dynamics and catalysis: Detection of segmental motion associated with rate-limiting product release by a glutathione transferase
    • Codreanu, S. G., Ladner, J. E., Xiao, G., Stourman, N. V., Hachey, D. L., Gilliland, G. L., and Armstrong, R. N. (2002) Local protein dynamics and catalysis: Detection of segmental motion associated with rate-limiting product release by a glutathione transferase, Biochemistry 41, 15161-15172.
    • (2002) Biochemistry , vol.41 , pp. 15161-15172
    • Codreanu, S.G.1    Ladner, J.E.2    Xiao, G.3    Stourman, N.V.4    Hachey, D.L.5    Gilliland, G.L.6    Armstrong, R.N.7
  • 32
    • 0029003807 scopus 로고
    • Crystal structure of a theta-class glutathione transferase
    • Wilce, M. C. J., Board, P. G., Feil, S. C., and Parker, M. W (1995) Crystal structure of a theta-class glutathione transferase, EMBO J. 14, 2133-2143.
    • (1995) EMBO J. , vol.14 , pp. 2133-2143
    • Wilce, M.C.J.1    Board, P.G.2    Feil, S.C.3    Parker, M.W.4
  • 34
    • 0029101750 scopus 로고
    • Evidence for an essential serine residue in the active site of the theta class glutathione transferases
    • Board, P. G., Coggan, M., Wilce, M. C. J., and Parker, M. W. (1995) Evidence for an essential serine residue in the active site of the theta class glutathione transferases, Biochem. J. 311, 247-250.
    • (1995) Biochem. J. , vol.311 , pp. 247-250
    • Board, P.G.1    Coggan, M.2    Wilce, M.C.J.3    Parker, M.W.4
  • 35
    • 0034708616 scopus 로고    scopus 로고
    • Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme
    • Jemth, P., and Mannervik, B. (2000) Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme, J. Biol. Chem. 275, 8618-8624.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8618-8624
    • Jemth, P.1    Mannervik, B.2
  • 37
    • 0028181442 scopus 로고
    • The Nuclear Magnetic Resonance Solution Structure of the Mixed Disulfide between Escherichia coli Glutaredoxin(C14S) and Glutathione
    • Bushweller, J. H., Billeter, M., Holmgren, A., and Wuthrich, K. (1994) The Nuclear Magnetic Resonance Solution Structure of the Mixed Disulfide between Escherichia coli Glutaredoxin(C14S) and Glutathione, J. Mol. Biol. 235, 1585-1597.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1585-1597
    • Bushweller, J.H.1    Billeter, M.2    Holmgren, A.3    Wuthrich, K.4
  • 38
    • 0035919812 scopus 로고    scopus 로고
    • Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases
    • Xia, B., Vlamis-Gardikas, A., Holmgren, A., Wright, P. E., and Dyson, H. J. (2001) Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases, J. Mol. Biol. 310, 907-918.
    • (2001) J. Mol. Biol. , vol.310 , pp. 907-918
    • Xia, B.1    Vlamis-Gardikas, A.2    Holmgren, A.3    Wright, P.E.4    Dyson, H.J.5


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