Structural basis for detoxification and oxidative stress protection in membranes

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Bibtex

@article{351ac7cf5cdd4638ad0e00131e006ae9,
title = "Structural basis for detoxification and oxidative stress protection in membranes",
abstract = "Synthesis of mediators of fever, pain and inflammation as well as protection against reactive molecules and oxidative stress is a hallmark of the MAPEG superfamily (membrane associated proteins in eicosanoid and glutathione metabolism). The structure of a MAPEG member, rat mictosomal glutathione transferase 1, at 3.2 angstrom resolution, solved here in complex with glutathione by electron crystallography, defines the active site location and a cytosolic domain involved in enzyme activation. The glutathione binding site is found to be different from that of the canonical soluble glutathione transferases. The architecture of the homotrimer supports a catalytic mechanism involving subunit interactions and reveals both cytosolic and membraneous substrate entry sites, providing a rationale for the membrane location of the enzyme.",
keywords = "electron crystallography, protein structure, enzymology, membrane protein, oxidative stress",
author = "Peter Holm and Priyaranjan Bhakat and Caroline Jegerschold and Nobuhiko Gyobu and Kaoru Mitsuoka and Yoshinori Fujiyoshi and Ralf Morgenstern and Hans Hebert",
year = "2006",
doi = "10.1016/j.jmb.2006.05.056",
language = "English",
volume = "360",
pages = "934--945",
journal = "Journal of Molecular Biology",
issn = "1089-8638",
publisher = "Elsevier",
number = "5",

}