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Volumn 273, Issue 4, 1997, Pages 857-872

Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola hepatica glutathione S-transferase

Author keywords

Crystallization; Detoxification; Fasciola; Glutathione S transferase; X ray crystallography

Indexed keywords

GLUTATHIONE TRANSFERASE; ISOENZYME; VACCINE;

EID: 0031558812     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1338     Document Type: Article
Times cited : (47)

References (62)
  • 1
    • 0028327862 scopus 로고
    • Glutathione S-transferases: Structure and mechanism of an archetypical detoxification enzyme
    • Armstrong R. N. Glutathione S-transferases: structure and mechanism of an archetypical detoxification enzyme. Advan. Enzymol. 69:1993;1-44.
    • (1993) Advan. Enzymol. , vol.69 , pp. 1-44
    • Armstrong, R.N.1
  • 2
    • 0023250405 scopus 로고
    • A purified 28,000 dalton protein fromSchistosoma mansoni
    • Balloul J. M., Grzych J-W., Pierce R. J., Capron A. A. A purified 28,000 dalton protein fromSchistosoma mansoni. J. Immunol. 138:1987;3448-3453.
    • (1987) J. Immunol. , vol.138 , pp. 3448-3453
    • Balloul, J.M.1    Grzych, J-W.2    Pierce, R.J.3    Capron, A.A.4
  • 3
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton G. J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 5
    • 0027992651 scopus 로고
    • Parasitic helminth glutathione S-transferases: An update on their potential as targets for immuno- And chemotherapy
    • Brophy P. M., Pritchard D. I. Parasitic helminth glutathione S-transferases: an update on their potential as targets for immuno- and chemotherapy. Expt. Parasitol. 79:1994;89-96.
    • (1994) Expt. Parasitol. , vol.79 , pp. 89-96
    • Brophy, P.M.1    Pritchard, D.I.2
  • 8
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A. T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992b;472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4
    • CCP4. 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
  • 10
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C., Lesk A. M. The relation between the divergence of sequence and structure in proteins. EMBO J. 5:1986;823-826.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 12
    • 0028224013 scopus 로고
    • X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function
    • Dirr H. W., Reinemer P., Huber R. X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function. Eur. J. Biochem. 220:1994a;645-661.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 645-661
    • Dirr, H.W.1    Reinemer, P.2    Huber, R.3
  • 13
    • 0028079744 scopus 로고
    • Refined crystal structure of porcine pi class glutathione S-transferase (pGST P1-1) at 2.1 Å resolution
    • Dirr H. W., Reinemer P., Huber R. Refined crystal structure of porcine pi class glutathione S-transferase (pGST P1-1) at 2.1 Å resolution. J. Mol. Biol. 243:1994b;72-92.
    • (1994) J. Mol. Biol. , vol.243 , pp. 72-92
    • Dirr, H.W.1    Reinemer, P.2    Huber, R.3
  • 14
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray structure refinement
    • Engh R. A., Huber R. Accurate bond and angle parameters for X-ray structure refinement. Acta Crystallog. sect.A. 47:1991;392-400.
    • (1991) Acta Crystallog. Sect.a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 15
    • 0023284539 scopus 로고
    • Production losses and control of helminths in ruminants of tropical regions
    • Fabiyi J. P. Production losses and control of helminths in ruminants of tropical regions. Int. J. Parasitol. 17:1987;435-442.
    • (1987) Int. J. Parasitol. , vol.17 , pp. 435-442
    • Fabiyi, J.P.1
  • 16
    • 0028218792 scopus 로고
    • Molecular structure at 1.8 Å of mouse liver class pi glutathione S-transferase complexed with S-(p
    • García-Sáez I., Párraga A., Philips M. F., Mantle T. J., Coll M. Molecular structure at 1.8 Å of mouse liver class pi glutathione S-transferase complexed with S-(p. J. Mol. Biol. 237:1994;298-314.
    • (1994) J. Mol. Biol. , vol.237 , pp. 298-314
    • García-Sáez, I.1    Párraga, A.2    Philips, M.F.3    Mantle, T.J.4    Coll, M.5
  • 17
    • 0000898340 scopus 로고
    • The biological macromolecule database, version 3.0: New features, data, and the NASA archive for protein crystal growth data
    • Gilliland G. L., Tung M., Blakeslee D. M., Ladner J. The biological macromolecule database, version 3.0: New features, data, and the NASA archive for protein crystal growth data. Acta Crystallog. sect. D. 50:1994;408-413.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 408-413
    • Gilliland, G.L.1    Tung, M.2    Blakeslee, D.M.3    Ladner, J.4
  • 18
    • 0022626336 scopus 로고
    • Resistance to fascioliasis: A review
    • Haroun E. M., Hillyer G. V. Resistance to fascioliasis: a review. Vet. Parasitol. 20:1986;63-93.
    • (1986) Vet. Parasitol. , vol.20 , pp. 63-93
    • Haroun, E.M.1    Hillyer, G.V.2
  • 19
    • 0012179965 scopus 로고
    • Glutathione S-transferases inFasciola hepatica
    • Howell M. J., Board P. J., Boray J. C. Glutathione S-transferases inFasciola hepatica. J. Parasitol. 74:1988;715-718.
    • (1988) J. Parasitol. , vol.74 , pp. 715-718
    • Howell, M.J.1    Board, P.J.2    Boray, J.C.3
  • 20
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF: A program to identify and analyse structural motifs in proteins
    • Hutchinson G. E., Thornton J. M. PROMOTIF: A program to identify and analyse structural motifs in proteins. Protein Sci. 5:1996;212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, G.E.1    Thornton, J.M.2
  • 21
    • 0026460365 scopus 로고
    • The three-dimensional structure of a glutathione S-transferase from the mu class gene. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution
    • Ji X., Zhang P., Armstrong R. N., Gilliland G. L. The three-dimensional structure of a glutathione S-transferase from the mu class gene. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution. Biochemistry. 31:1992;10169-10184.
    • (1992) Biochemistry , vol.31 , pp. 10169-10184
    • Ji, X.1    Zhang, P.2    Armstrong, R.N.3    Gilliland, G.L.4
  • 23
    • 0028218381 scopus 로고
    • Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the dia stereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene
    • Ji X., Johnson W. W., Sesay M. A., Dickert L., Prasad S. M., Ammon H. L., Armstrong R. N., Gilliland G. L. Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the dia stereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene. Biochemistry. 33:1994;1043-1052.
    • (1994) Biochemistry , vol.33 , pp. 1043-1052
    • Ji, X.1    Johnson, W.W.2    Sesay, M.A.3    Dickert, L.4    Prasad, S.M.5    Ammon, H.L.6    Armstrong, R.N.7    Gilliland, G.L.8
  • 24
    • 0029064985 scopus 로고
    • Three dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods
    • Ji X., von Rosenvinge E. C., Johnson W. W., Tomarev S. I., Piatigorsky J., Armstrong R. N., Gilliland G. L. Three dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Biochemistry. 34:1995;5317-5328.
    • (1995) Biochemistry , vol.34 , pp. 5317-5328
    • Ji, X.1    Von Rosenvinge, E.C.2    Johnson, W.W.3    Tomarev, S.I.4    Piatigorsky, J.5    Armstrong, R.N.6    Gilliland, G.L.7
  • 25
    • 0029776028 scopus 로고    scopus 로고
    • Location of a potential transport binding site in sigma class glutathione transferase by X-ray crystallography
    • Ji X., von Rosenvinge E. C., Johnson W. W., Armstrong R. N., Gilliland G. L. Location of a potential transport binding site in sigma class glutathione transferase by X-ray crystallography. Proc. Natl Acad. Sci. USA, 93:1996;8208-8213.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8208-8213
    • Ji, X.1    Von Rosenvinge, E.C.2    Johnson, W.W.3    Armstrong, R.N.4    Gilliland, G.L.5
  • 26
    • 0027241006 scopus 로고
    • Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of glutathione S-transferase
    • Johnson W. W., Liu S., Ji X., Gilliland G. L., Armstrong R. N. Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of glutathione S-transferase. J. Biol. Chem. 268:1993;11508-11511.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11508-11511
    • Johnson, W.W.1    Liu, S.2    Ji, X.3    Gilliland, G.L.4    Armstrong, R.N.5
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of proteins
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of proteins. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 0023046955 scopus 로고
    • Cloning and sequence analysis of a cDNA from a rat liver glutathione S-transferase Yb subunit
    • Lai H. C., Grove G., Tu C. P. Cloning and sequence analysis of a cDNA from a rat liver glutathione S-transferase Yb subunit. Nucl. Acids Res. 14:1986;6101-6114.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 6101-6114
    • Lai, H.C.1    Grove, G.2    Tu, C.P.3
  • 31
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArthur M. W., Moss D. S., 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
  • 33
    • 0002123353 scopus 로고
    • Gluathione S-transferases: Intracellular binding, detoxification, and adaptive responses
    • N. Tavolini, & P.D. Beck. New York: Raven Press
    • Listowski I. Gluathione S-transferases: intracellular binding, detoxification, and adaptive responses. Tavolini N., Beck P. D. Hepatic Transport and Bile Secretion: Physiology and Pathaphysiology. 1993;Raven Press, New York.
    • (1993) Hepatic Transport and Bile Secretion: Physiology and Pathaphysiology
    • Listowski, I.1
  • 34
    • 0026610767 scopus 로고
    • Assessment of protein models with 3-dimensional profiles
    • Lüthy R., Bowie J. U., Eisenberg D. Assessment of protein models with 3-dimensional profiles. Nature. 356:1992;83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 36
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B. W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 38
    • 0028931691 scopus 로고
    • Crystal structures of a schistosomal drug and vaccine target: Glutathione S-transferase fromSchistosoma japonicum
    • McTigue M., Williams D. R., Tainer J. A. Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase fromSchistosoma japonicum. J. Mol. Biol. 246:1995;21-27.
    • (1995) J. Mol. Biol. , vol.246 , pp. 21-27
    • McTigue, M.1    Williams, D.R.2    Tainer, J.A.3
  • 41
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. D. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 157-163
    • Navaza, J.1
  • 42
    • 0026319199 scopus 로고
    • Protein folding and Association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K. A., Honig B. Protein folding and Association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 43
    • 0031017331 scopus 로고    scopus 로고
    • The three-dimensional structure of the human pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate
    • Oakley A. J., Rossjohn J., Bello M. L., Caccuri A. M., Federici G., Parker M. W. The three-dimensional structure of the human pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate. Biochemistry. 36:1997;576-585.
    • (1997) Biochemistry , vol.36 , pp. 576-585
    • Oakley, A.J.1    Rossjohn, J.2    Bello, M.L.3    Caccuri, A.M.4    Federici, G.5    Parker, M.W.6
  • 44
    • 0003976860 scopus 로고
    • Data collection and processing
    • Sawyer, L.Issacs, N.Bailey, S. SERC, Daresbury Laboratory, UK
    • Otwinowski, Z. 1993, Data collection and processing, Proceedings of the CCP4 Study Weekend, Sawyer, L.Issacs, N.Bailey, S. SERC, Daresbury Laboratory, UK.
    • (1993) Proceedings of the CCP4 Study Weekend
    • Otwinowski, Z.1
  • 45
    • 0026827506 scopus 로고
    • Molecular characterisation of cDNA sequences encoding glutathione S-transferases fromFasciola hepatica
    • Panaccio M., Wilson L. R., Crameri S. L., Wijffels G. L., Spithill T. W. Molecular characterisation of cDNA sequences encoding glutathione S-transferases fromFasciola hepatica. Exp. Parasitol. 74:1992;232-237.
    • (1992) Exp. Parasitol. , vol.74 , pp. 232-237
    • Panaccio, M.1    Wilson, L.R.2    Crameri, S.L.3    Wijffels, G.L.4    Spithill, T.W.5
  • 46
    • 0029854518 scopus 로고    scopus 로고
    • Glutathione S-transferase class Kappa: Characterisation by the cloning of the rat mitochondrial GST and identification of a human homologue
    • Pemble S. E., Wardle A. F., Taylor J. B. Glutathione S-transferase class Kappa: characterisation by the cloning of the rat mitochondrial GST and identification of a human homologue. Biochem. J. 319:1996;749-754.
    • (1996) Biochem. J. , vol.319 , pp. 749-754
    • Pemble, S.E.1    Wardle, A.F.2    Taylor, J.B.3
  • 47
    • 0028244183 scopus 로고
    • Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity
    • Raghunathan S., Chandross R. J., Kretsinger R. H., Allison T. J., Penington C. J., Rule G. S. Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity. J. Mol. Biol. 238:1994;815-832.
    • (1994) J. Mol. Biol. , vol.238 , pp. 815-832
    • Raghunathan, S.1    Chandross, R.J.2    Kretsinger, R.H.3    Allison, T.J.4    Penington, C.J.5    Rule, G.S.6
  • 48
    • 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
  • 49
    • 0025816448 scopus 로고
    • The three-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution
    • Reinemer P., Dirr H. W., Ladenstein R., Schaffer J., Gallay O., Huber R. The three-dimensional structure of class π glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO J. 10:1991;1997-2005.
    • (1991) EMBO J. , vol.10 , pp. 1997-2005
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Schaffer, J.4    Gallay, O.5    Huber, R.6
  • 50
    • 0026722795 scopus 로고
    • Three dimensional structure of class π glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution
    • Reinemer P., Dirr H. W., Ladenstein R., Huber R., Lo Bello M., Federici G., Parker M. W. Three dimensional structure of class π glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution. J. Mol. Biol. 227:1992;214-226.
    • (1992) J. Mol. Biol. , vol.227 , pp. 214-226
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Huber, R.4    Lo Bello, M.5    Federici, G.6    Parker, M.W.7
  • 52
    • 0030010730 scopus 로고    scopus 로고
    • A structurally derived consensus pattern for the theta class glutathione transferases
    • Rossjohn J., Board P. G., Parker M. W., Wilce M. C. J. A structurally derived consensus pattern for the theta class glutathione transferases. Protein Eng. 9:1996;327-332.
    • (1996) Protein Eng. , vol.9 , pp. 327-332
    • Rossjohn, J.1    Board, P.G.2    Parker, M.W.3    Wilce, M.C.J.4
  • 58
    • 0026538493 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of a protective cloned 28 kDa glutathione S-transferase fromSchistosoma mansoni
    • Trottein F., Vaney M. C., Bachet B., Pierce R. J., Colloc'h N., Lecocq J. P., Capron A., Mornon J. P. Crystallization and preliminary X-ray diffraction studies of a protective cloned 28 kDa glutathione S-transferase fromSchistosoma mansoni. J. Mol. Biol. 224:1992;515-518.
    • (1992) J. Mol. Biol. , vol.224 , pp. 515-518
    • Trottein, F.1    Vaney, M.C.2    Bachet, B.3    Pierce, R.J.4    Colloc'H, N.5    Lecocq, J.P.6    Capron, A.7    Mornon, J.P.8
  • 59
    • 0025778535 scopus 로고
    • Cloning, expression and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus
    • Voracheck W. R., Pearson R. W., Rule G. S. Cloning, expression and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus. Proc. Natl Acad. Sci. USA. 88:1991;4443-4447.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 4443-4447
    • Voracheck, W.R.1    Pearson, R.W.2    Rule, G.S.3
  • 61
    • 0028263070 scopus 로고
    • Structure and function of glutathione S-transferases
    • Wilce M. C. J., Parker M. W. Structure and function of glutathione S-transferases. Biochim. Biophys. Acta. 1205:1994;1-18.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 1-18
    • Wilce, M.C.J.1    Parker, M.W.2
  • 62
    • 0029003807 scopus 로고
    • Crystal structure of a theta-class glutathione transferase
    • Wilce M. C. J., Board P. G., Feil S. C., Parker M. W. Crystal structure of a theta-class glutathione transferase. EMBO J. 14:1995;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


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