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Structural basis for detoxification and oxidative stress protection in membranes.

Authors: Holm, PJ  Bhakat, P  Jegerschold, C  Gyobu, N  Mitsuoka, K  Fujiyoshi, Y  Morgenstern, R  Hebert, H 
Citation: Holm PJ, etal., J Mol Biol. 2006 Jul 28;360(5):934-45. Epub 2006 Jun 5.
Pubmed: (View Article at PubMed) PMID:16806268
DOI: Full-text: DOI:10.1016/j.jmb.2006.05.056

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.

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RGD Object Information
RGD ID: 8553629
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.