Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4

The mammalian glutathione peroxidase (GPx) family is a key component of the cellular antioxidative defence system. Within this family, GPx4 has unique features as it accepts a large class of hydroperoxy lipid substrates and has a plethora of biological functions, including sperm maturation, regulati...

Descripción completa

Detalles Bibliográficos
Autores principales: Janowski, Robert, Scanu, Sandra, Niessing, Dierk, Madl, Tobias
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2016
Materias:
Research Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5053159/
https://www.ncbi.nlm.nih.gov/pubmed/27710939
http://dx.doi.org/10.1107/S2053230X16013686
_version_ 1782458359878778880
author Janowski, Robert
Scanu, Sandra
Niessing, Dierk
Madl, Tobias
author_facet Janowski, Robert
Scanu, Sandra
Niessing, Dierk
Madl, Tobias
author_sort Janowski, Robert
collection PubMed
description The mammalian glutathione peroxidase (GPx) family is a key component of the cellular antioxidative defence system. Within this family, GPx4 has unique features as it accepts a large class of hydroperoxy lipid substrates and has a plethora of biological functions, including sperm maturation, regulation of apoptosis and cerebral embryogenesis. In this paper, the structure of the cytoplasmic isoform of mouse phospholipid hydroperoxide glutathione peroxidase (O70325-2 GPx4) with selenocysteine 46 mutated to cysteine is reported solved at 1.8 Å resolution using X-ray crystallography. Furthermore, solution data of an isotope-labelled GPx protein are presented.
format Online
Article
Text
id pubmed-5053159
institution National Center for Biotechnology Information
language English
publishDate 2016
publisher International Union of Crystallography
record_format MEDLINE/PubMed
spelling pubmed-50531592016-10-13 Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4 Janowski, Robert Scanu, Sandra Niessing, Dierk Madl, Tobias Acta Crystallogr F Struct Biol Commun Research Communications The mammalian glutathione peroxidase (GPx) family is a key component of the cellular antioxidative defence system. Within this family, GPx4 has unique features as it accepts a large class of hydroperoxy lipid substrates and has a plethora of biological functions, including sperm maturation, regulation of apoptosis and cerebral embryogenesis. In this paper, the structure of the cytoplasmic isoform of mouse phospholipid hydroperoxide glutathione peroxidase (O70325-2 GPx4) with selenocysteine 46 mutated to cysteine is reported solved at 1.8 Å resolution using X-ray crystallography. Furthermore, solution data of an isotope-labelled GPx protein are presented. International Union of Crystallography 2016-09-22 /pmc/articles/PMC5053159/ /pubmed/27710939 http://dx.doi.org/10.1107/S2053230X16013686 Text en © Janowski et al. 2016 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Research Communications
Janowski, Robert
Scanu, Sandra
Niessing, Dierk
Madl, Tobias
Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4
title Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4
title_full Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4
title_fullStr Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4
title_full_unstemmed Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4
title_short Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4
title_sort crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5053159/
https://www.ncbi.nlm.nih.gov/pubmed/27710939
http://dx.doi.org/10.1107/S2053230X16013686
work_keys_str_mv AT janowskirobert crystalandsolutionstructuralstudiesofmousephospholipidhydroperoxideglutathioneperoxidase4
AT scanusandra crystalandsolutionstructuralstudiesofmousephospholipidhydroperoxideglutathioneperoxidase4
AT niessingdierk crystalandsolutionstructuralstudiesofmousephospholipidhydroperoxideglutathioneperoxidase4
AT madltobias crystalandsolutionstructuralstudiesofmousephospholipidhydroperoxideglutathioneperoxidase4

Ejemplares similares