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Electron Crystallography of a Small Membrane-Bound Enzyme, Microsomal Glutathione Transferase

Published online by Cambridge University Press:  02 July 2020

Hans Hebert
Affiliation:
Department of Biosciences, Karolinska Institutet, Novum, S-141 57 Huddinge, Sweden
Ingeborg Schmidt-Krey
Affiliation:
Department of Biosciences, Karolinska Institutet, Novum, S-141 57 Huddinge, Sweden Present address: Harvard Medical School, Dept. of Cell Biology, 240 Longwood Avenue, Boston, MA02115
Kaoru Mitsuoka
Affiliation:
Department of Biophysics, Faculty of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, 606-01, Japan
Teruhisa Hirai
Affiliation:
Laboratory of Ultrastructure Research, National Institute for Physiological Sciences, Myodaiji-cho, Okazaki, 444-8585Japan
Kazuyoshi Murata
Affiliation:
Laboratory of Ultrastructure Research, National Institute for Physiological Sciences, Myodaiji-cho, Okazaki, 444-8585Japan
Yifan Cheng
Affiliation:
Department of Biosciences, Karolinska Institutet, Novum, S-141 57 Huddinge, Sweden Present address: Harvard Medical School, Dept. of Cell Biology, 240 Longwood Avenue, Boston, MA02115
Yoshinori Fujiyoshi
Affiliation:
Laboratory of Ultrastructure Research, National Institute for Physiological Sciences, Myodaiji-cho, Okazaki, 444-8585Japan
Ralf Morgenstern
Affiliation:
Laboratory of Ultrastructure Research, National Institute for Physiological Sciences, Myodaiji-cho, Okazaki, 444-8585Japan
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Extract

Microsomal glutathione transferase 1, MGST1, belongs to a recently characterised superfamily named MAPEG (membrane associated proteins in eicosanoid and glutathione metabolism) which has evolved divergent functions to protect against reactive lipid intermediates (lipid hydroperoxides and hydroxyalkenals) or indeed harness these molecules for key physiological functions (leukotrienes and prostaglandins). The most thoroughly studied member of this superfamily is MGST1 which is an abundant detoxication enzyme displaying both glutathione transferase and peroxidase activities.

The MGST1 monomer has a molecular mass of 17.5 kD and three to four transmembrane regions can be localized from hydropathy plots (Fig. 1). One transmembrane stretch was shown by trypsin cleavage to be situated between lysine-4 and lysine-41 with the N-terminal on the lumenal side of the membrane. The active site is located on the cytoplasmic side of the endoplasmic reticulum.

Type
Electron Cryomicroscopy of Macromolecules
Copyright
Copyright © Microscopy Society of America

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References

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