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Structural basis for detoxification and oxidative stress protection in membranes
Authors:Holm Peter J  Bhakat Priyaranjan  Jegerschöld Caroline  Gyobu Nobuhiko  Mitsuoka Kaoru  Fujiyoshi Yoshinori  Morgenstern Ralf  Hebert Hans
Institution:Department of Biosciences and Nutrition, Karolinska Institutet and School of Technology and Health, Royal Institute of Technology, SE-14157 Huddinge, Sweden.
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 microsomal glutathione transferase 1, at 3.2 A 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:GST  glutathione transferase  MAPEG  membrane associated proteins in eicosanoid and glutathione metabolism  MGST1  microsomal glutathione transferase 1  GSH  tri-peptide glutathione
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