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Structural basis for detoxification and oxidative stress protection in membranes

Holm, Peter LU ; Bhakat, Priyaranjan; Jegerschold, Caroline; Gyobu, Nobuhiko; Mitsuoka, Kaoru; Fujiyoshi, Yoshinori; Morgenstern, Ralf and Hebert, Hans LU (2006) In Journal of Molecular Biology 360(5). p.934-945
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
electron crystallography, protein structure, enzymology, membrane protein, oxidative stress
in
Journal of Molecular Biology
volume
360
issue
5
pages
934 - 945
publisher
Elsevier
external identifiers
  • wos:000239670200002
  • pmid:16806268
  • scopus:33745938162
ISSN
1089-8638
DOI
10.1016/j.jmb.2006.05.056
language
English
LU publication?
yes
id
351ac7cf-5cdd-4638-ad0e-00131e006ae9 (old id 398388)
date added to LUP
2007-08-20 15:40:54
date last changed
2019-10-20 04:14:20
@article{351ac7cf-5cdd-4638-ad0e-00131e006ae9,
  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.},
  author       = {Holm, Peter and Bhakat, Priyaranjan and Jegerschold, Caroline and Gyobu, Nobuhiko and Mitsuoka, Kaoru and Fujiyoshi, Yoshinori and Morgenstern, Ralf and Hebert, Hans},
  issn         = {1089-8638},
  keyword      = {electron crystallography,protein structure,enzymology,membrane protein,oxidative stress},
  language     = {eng},
  number       = {5},
  pages        = {934--945},
  publisher    = {Elsevier},
  series       = {Journal of Molecular Biology},
  title        = {Structural basis for detoxification and oxidative stress protection in membranes},
  url          = {http://dx.doi.org/10.1016/j.jmb.2006.05.056},
  volume       = {360},
  year         = {2006},
}