Reference : Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/38218
Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2
English
Smeets, Aude [Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Structurale (CSTR) > >]
Evrard, Christine mailto [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 mailto [Université Catholique de Louvain - UCL > > Institut des sciences de la vie - ISV > >]
Declercq, Jean-Paul mailto [Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Structurale (CSTR) > >]
2005
Protein Science : A Publication of the Protein Society
Cold Spring Harbor Laboratory Press
14
2610-2621
Yes (verified by ORBi)
International
0961-8368
1469-896X
Woodbury
NY
[en] human thioredoxin ; X-ray crystal structure ; mitochondria ; oxidized state ; reduced state
[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.
http://hdl.handle.net/2268/38218

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