ORBi: Smeets Aude - Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2

Reference : Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/38218

Title :	Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2
Language :	English
Author, co-author :	Smeets, Aude [Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Structurale (CSTR) > >]
	Evrard, Christine [Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Structurale (CSTR) > >]
	Landtmeters, Marie [Université Catholique de Louvain - UCL > > Institut des sciences de la vie - ISV > >]
	Marchand, Cécile [Université Catholique de Louvain - UCL > > Institut des sciences de la vie - ISV > >]
	Knoops, Bernard [Université Catholique de Louvain - UCL > > Institut des sciences de la vie - ISV > >]
	Declercq, Jean-Paul [Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Structurale (CSTR) > >]
Publication date :	2005
Journal title :	Protein Science : A Publication of the Protein Society
Publisher :	Cold Spring Harbor Laboratory Press
Volume :	14
Pages :	2610-2621
Audience :	International
ISSN :	0961-8368
e-ISSN :	1469-896X
City :	Woodbury
Country :	NY
Keywords :	[en] human thioredoxin ; X-ray crystal structure ; mitochondria ; oxidized state ; reduced state
Abstract :	[en] Mammalian thioredoxin 2 is a mitochondrial isoform of highly evolutionary conserved thioredoxins. Thioredoxins are small ubiquitous protein–disulfide oxidoreductases implicated in a large variety of biological functions. In mammals, thioredoxin 2 is encoded by a nuclear gene and is targeted to mitochondria by a N-terminal mitochondrial presequence. Recently, mitochondrial thioredoxin 2 was shown to interact with components of the mitochondrial respiratory chain and to play a role in the control of mitochondrial membrane potential, regulating mitochondrial apoptosis signaling pathway. Here we report the first crystal structures of a mammalian mitochondrial thioredoxin 2. Crystal forms of reduced and oxidized human thioredoxin 2 are described at 2.0 and 1.8A ˚ resolution. Though the folding is rather similar to that of human cytosolic/nuclear thioredoxin 1, important differences are observed during the transition between the oxidized and the reduced states of human thioredoxin 2, compared with human thioredoxin 1. In spite of the absence of the Cys residue implicated in dimer formation in human thioredoxin 1, dimerization still occurs in the crystal structure of human thioredoxin 2, mainly mediated by hydrophobic contacts, and the dimers are associated to form two-dimensional polymers. Interestingly, the structure of human thioredoxin 2 reveals possible interaction domains with human peroxiredoxin 5, a substrate protein of human thioredoxin 2 in mitochondria.
Permalink :	http://hdl.handle.net/2268/38218

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