Structural basis for detoxification and oxidative stress protection in membranes
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/398388
- author
- Holm, Peter LU ; Bhakat, Priyaranjan ; Jegerschold, Caroline ; Gyobu, Nobuhiko ; Mitsuoka, Kaoru ; Fujiyoshi, Yoshinori ; Morgenstern, Ralf and Hebert, Hans LU
- organization
- publishing date
- 2006
- 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
- pmid:16806268
- 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
- 2016-04-01 15:27:11
- date last changed
- 2022-04-22 07:47:35
@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}}, keywords = {{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}}, doi = {{10.1016/j.jmb.2006.05.056}}, volume = {{360}}, year = {{2006}}, }