Structural basis for detoxification and oxidative stress protection in membranes

Holm, Peter (author): Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH

Bhakat, Priyaranjan (author)

Gyobu, Nobuhiko (author)

Mitsuoka, Kaoru (author)

Fujiyoshi, Yoshinori (author)

Hebert, Hans (author): Karolinska Institutet,Lund University,Lunds universitet,KTH,Strukturell bioteknik,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH

(creator_code:org_t)

Elsevier BV, 2006
2006
English.
In: Journal of Molecular Biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 360:5, s. 934-945

Related links:: http://dx.doi.org/10...; show more...; https://urn.kb.se/re...; https://doi.org/10.1...; https://lup.lub.lu.s...; http://kipublication...; show less...

Abstract Subject headings

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.

By the author/editor: Holm, Peter; Bhakat, Priyaran ...; Jegerschold, Car ...; Gyobu, Nobuhiko; Mitsuoka, Kaoru; Fujiyoshi, Yoshi ...; show more...; Morgenstern, Ral ...; Hebert, Hans; show less...

About the subject

By the university: Royal Institute of Technology; Lund University; Karolinska Institutet

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.