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Volumn 271, Issue 5, 1997, Pages 751-758

The 3.0 Å projection structure of microsomal glutathione transferase as determined by electron crystallography of p21212 two-dimensional crystals

Author keywords

Detoxification; Electron microscopy; Membrane protein; Microsomal glutathione transferase; Two dimensional crystallization

Indexed keywords

GLUTATHIONE TRANSFERASE; PHOSPHOLIPID;

EID: 0031554721     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1216     Document Type: Article
Times cited : (39)

References (37)
  • 2
    • 0025971827 scopus 로고
    • Glutathione S-transferases: Reaction mechanism, structure, and function
    • Armstrong, R. N. (1991). Glutathione S-transferases: reaction mechanism, structure, and function. Chem. Res. Toxicol. 4, 131-140.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 131-140
    • Armstrong, R.N.1
  • 3
    • 0024278917 scopus 로고
    • Images of purple membrane at 2.8 Å resolution obtained by cryo-electron microscopy
    • Baldwin, J. M., Henderson, R., Beckman, E. & Zemlin, F. (1988). Images of purple membrane at 2.8 Å resolution obtained by cryo-electron microscopy. J. Mol. Biol. 202, 585-591.
    • (1988) J. Mol. Biol. , vol.202 , pp. 585-591
    • Baldwin, J.M.1    Henderson, R.2    Beckman, E.3    Zemlin, F.4
  • 4
    • 0025228968 scopus 로고
    • The role of glutathione and glutathione transferases in chemical carcinogenesis
    • Coles, B. & Ketterer, B. (1990). The role of glutathione and glutathione transferases in chemical carcinogenesis. CRC Crit. Rev. Biochem. Mol. Biol. 25, 47-70.
    • (1990) CRC Crit. Rev. Biochem. Mol. Biol. , vol.25 , pp. 47-70
    • Coles, B.1    Ketterer, B.2
  • 7
    • 0028224013 scopus 로고
    • X-ray crystal structures of cytosolic glutathione S-transferases: Implications for protein architecture, substrate recognition and catalytic function
    • Dirr, H., Reinemer, P. & Huber, R. (1994). X-ray crystal structures of cytosolic glutathione S-transferases: implications for protein architecture, substrate recognition and catalytic function. Eur. J. Biochem. 220, 645-661.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 645-661
    • Dirr, H.1    Reinemer, P.2    Huber, R.3
  • 9
    • 0001312197 scopus 로고
    • Biological macromolecules observed with high resolution cryo-electron microscope
    • Imura, T., Maruse, S. & Suzuki, T., eds, The Japanese Society of Electron Microscopy, Tokyo, Japan
    • Fujiyoshi, Y., Uyeda, N., Yamagishi, H., Morikawa, K., Mizusaki, T., Aoki, Y., Kihara, H. & Harada, Y. (1986). Biological macromolecules observed with high resolution cryo-electron microscope. In Proceedings XIth International Congress on Electron Microscopy (Imura, T., Maruse, S. & Suzuki, T., eds), pp. 1829-1832, The Japanese Society of Electron Microscopy, Tokyo, Japan.
    • (1986) Proceedings XIth International Congress on Electron Microscopy , pp. 1829-1832
    • Fujiyoshi, Y.1    Uyeda, N.2    Yamagishi, H.3    Morikawa, K.4    Mizusaki, T.5    Aoki, Y.6    Kihara, H.7    Harada, Y.8
  • 12
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes, J. D. & Pulford, D. J. (1995). The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. CRC Crit. Rev. Biochem. Mol. Biol. 30, 445-600.
    • (1995) CRC Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 13
    • 0029082813 scopus 로고
    • The projection structure of microsomal glutathione transferase
    • Hebert, H., Schmidt-Krey, I. & Morgenstern, R. (1995). The projection structure of microsomal glutathione transferase. EMBO J. 14, 3864-3869.
    • (1995) EMBO J. , vol.14 , pp. 3864-3869
    • Hebert, H.1    Schmidt-Krey, I.2    Morgenstern, R.3
  • 14
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5 Å resolution
    • Henderson, R., Baldwin, J. M., Downing, K. H., Lepault, J. & Zemlin, F. (1986). Structure of purple membrane from Halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 Å resolution. Ultramicroscopy, 19,147-178.
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5
  • 15
    • 0025292355 scopus 로고
    • A model for the structure of bacteriorhodopsin based on high resolution electron crystallography
    • Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckman, E. & Downing, K. H. (1990). A model for the structure of bacteriorhodopsin based on high resolution electron crystallography. J. Mol. Biol. 213, 899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckman, E.5    Downing, K.H.6
  • 16
    • 0029107529 scopus 로고
    • Characterization of the safener-induced glutathione S-transferase isoform II from maize
    • Holt, D. C., Lay, V. J., Clarke, E. D., Dinsmore, A., Jepson, I., Bright, S. W. & Greenland, A. J. (1995). Characterization of the safener-induced glutathione S-transferase isoform II from maize. Planta, 196, 295-302.
    • (1995) Planta , vol.196 , pp. 295-302
    • Holt, D.C.1    Lay, V.J.2    Clarke, E.D.3    Dinsmore, A.4    Jepson, I.5    Bright, S.W.6    Greenland, A.J.7
  • 18
    • 0026460365 scopus 로고
    • A three-dimensional structure of a glutathione S-transferase from the mu gene class. 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. (1992). A three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2 Å resolution. Biochemistry, 31, 10169-10184.
    • (1992) Biochemistry , vol.31 , pp. 10169-10184
    • Ji, X.1    Zhang, P.2    Armstrong, R.N.3    Gilliland, G.L.4
  • 19
    • 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. H., Vonrosenvinge, E. C., Johnson, W. W., Tomarev, S. I., Piatigorsky, J., Armstrong, R. N. & Gilliland, G. L. (1995). 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, 5317-5328.
    • (1995) Biochemistry , vol.34 , pp. 5317-5328
    • Ji, X.H.1    Vonrosenvinge, E.C.2    Johnson, W.W.3    Tomarev, S.I.4    Piatigorsky, J.5    Armstrong, R.N.6    Gilliland, G.L.7
  • 21
    • 0022085013 scopus 로고
    • Secondary structure of a channel-forming protein: Porin from E. coli outer membranes
    • Kleffel, B., Garavito, R. M., Baumeister, W. & Rosenbusch, J. P. (1985). Secondary structure of a channel-forming protein: porin from E. coli outer membranes. EMBO J. 4, 1589-1592.
    • (1985) EMBO J. , vol.4 , pp. 1589-1592
    • Kleffel, B.1    Garavito, R.M.2    Baumeister, W.3    Rosenbusch, J.P.4
  • 22
    • 0028147508 scopus 로고
    • Atomic model of the plant light-harvesting complex by electron crystallography
    • Kühlbrandt, W., Wang, D. N. & Fujiyoshi, Y. (1994). Atomic model of the plant light-harvesting complex by electron crystallography. Nature, 367, 614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 23
    • 0024269217 scopus 로고
    • Glutathione transferases- structure and catalytic activity
    • Mannervik, B. & Danielson, U. H. (1988). Glutathione transferases-structure and catalytic activity. CRC Crit. Rev. Biochem. 23, 283-337.
    • (1988) CRC Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 26
    • 0020209472 scopus 로고
    • Microsomal glutathione transferase. Purification, initial characterization and demonstration that it is not identical to the cytosolic glutathione transferases A, B and C
    • Morgenstern, R., Guthenberg, C. & DePierre, J. W. (1982). Microsomal glutathione transferase. Purification, initial characterization and demonstration that it is not identical to the cytosolic glutathione transferases A, B and C. Eur. J. Biochem. 128,243-248.
    • (1982) Eur. J. Biochem. , vol.128 , pp. 243-248
    • Morgenstern, R.1    Guthenberg, C.2    DePierre, J.W.3
  • 27
    • 0021677474 scopus 로고
    • The distribution of microsomal glutathione transferase among different organelles, different organs and different organisms
    • Morgenstern, R., Lundqvist, G., Andersson, G., Balk, L. & DePierre, J. W. (1984). The distribution of microsomal glutathione transferase among different organelles, different organs and different organisms. biochem. Pharmacol. 33, 3609-3614.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 3609-3614
    • Morgenstern, R.1    Lundqvist, G.2    Andersson, G.3    Balk, L.4    DePierre, J.W.5
  • 29
    • 0026470986 scopus 로고
    • An evolutionary perspective on glutathione transferases inferred from class-theta glutathione transferase cDNA sequences
    • Pemble, S. E. & Taylor, J. B. (1992). An evolutionary perspective on glutathione transferases inferred from class-theta glutathione transferase cDNA sequences. Biochem. J. 287, 957-963.
    • (1992) Biochem. J. , vol.287 , pp. 957-963
    • Pemble, S.E.1    Taylor, J.B.2
  • 30
    • 0030296348 scopus 로고    scopus 로고
    • Membrane topology of recombinant rat liver microsomal glutathione transferase expressed in E. coli
    • Raza, H., Weinander, R., Ekström, L. & Morgenstern, R. (1996). Membrane topology of recombinant rat liver microsomal glutathione transferase expressed in E. coli. Biochem Biophys. Res. Commun. 228, 165-170.
    • (1996) Biochem Biophys. Res. Commun. , vol.228 , pp. 165-170
    • Raza, H.1    Weinander, R.2    Ekström, L.3    Morgenstern, R.4
  • 31
    • 0025816448 scopus 로고
    • The three-dimensional structure of class-pi 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. (1991). The three-dimensional structure of class-pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO J. 10, 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
  • 32
    • 0026722795 scopus 로고
    • Three-dimensional structure of class n glutathione S-transferase from human placenta in complex with S-hexyglutathione at 2.8 Å resolution
    • Reinemer, P., Dirr, H. W., Ladenstein, R., Huber, R., Lo Bello, M., Federici, G. & Parker, M. W. (1992). Three-dimensional structure of class n glutathione S-transferase from human placenta in complex with S-hexyglutathione at 2.8 Å resolution. J. Mol. Biol. 227, 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
  • 34
    • 0028106016 scopus 로고
    • Glutathione-associated enzymes in anticancer drug resistance
    • Tew, K. D. (1994). Glutathione-associated enzymes in anticancer drug resistance. Cancer Res. 54, 4314-4320.
    • (1994) Cancer Res. , vol.54 , pp. 4314-4320
    • Tew, K.D.1
  • 35
    • 0026061928 scopus 로고
    • High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media
    • Wang, D. N. & Kühlbrandt, W. (1991). High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media. J. Mol. Biol. 217, 691-699.
    • (1991) J. Mol. Biol. , vol.217 , pp. 691-699
    • Wang, D.N.1    Kühlbrandt, W.2
  • 37
    • 0030911870 scopus 로고    scopus 로고
    • Structural and functional aspects of rat microsomal glutathione transferase: The roles of cysteine-49, arginine-107, lysine-67, histidine and tyrosine residues
    • In the press
    • Weinander, R., Ekström, L., Andersson, C., Raza, H., Bergman, T. & Morgenstern, R. (1997). Structural and functional aspects of rat microsomal glutathione transferase: the roles of cysteine-49, arginine-107, lysine-67, histidine and tyrosine residues. J. Biol. Chem. In the press.
    • (1997) J. Biol. Chem.
    • Weinander, R.1    Ekström, L.2    Andersson, C.3    Raza, H.4    Bergman, T.5    Morgenstern, R.6


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