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TitleStructural basis for detoxification and oxidative stress protection in membranes.
Journal, issue, pagesJ Mol Biol, Vol. 360, Issue 5, Page 934-945, Year 2006
Publish dateJul 28, 2006
AuthorsPeter J Holm / Priyaranjan Bhakat / Caroline Jegerschöld / Nobuhiko Gyobu / Kaoru Mitsuoka / Yoshinori Fujiyoshi / Ralf Morgenstern / Hans Hebert /
PubMed AbstractSynthesis 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 ...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.
External linksJ Mol Biol / PubMed:16806268
MethodsEM (electron crystallography)
Resolution3.2 Å
Structure data

PDB-2h8a:
Structure of Microsomal Glutathione Transferase 1 in Complex with Glutathione
Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 3.2 Å

Chemicals

ChemComp-GSH:
GLUTATHIONE

Source
  • rattus norvegicus (Norway rat)
KeywordsTRANSFERASE / Membrane protein

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