Reference : Crystal structure of the C47S mutant of human peroxiredoxin 5
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/57221
Crystal structure of the C47S mutant of human peroxiredoxin 5
English
Evrard, Christine mailto [Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Structurale (CSTR) > >]
Smeets, Aude [Université Catholique de Louvain - UCL > Département de Chimie > Unité de Chimie Structurale (CSTR) > >]
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) > >]
2004
Journal of Chemical Crystallography
Springer Science & Business Media B.V.
34
553-558
Yes (verified by ORBi)
International
1074-1542
[en] Antioxidant enzyme ; peroxiredoxin ; thioredoxin fold ; thioredoxin peroxidase
[en] In the crystal structure of the reduced form of the wild-type human peroxiredoxin 5, the
presence of a benzoate ion in direct interaction with the peroxidatic cysteine (Cys 47) appeared
as a rather intriguing feature since it is known that the benzoate ion can play the
role of a specific hydroxyl radical scavenger. The crystal structure of the C47S mutant of
the same enzyme has been crystallized in the tetragonal system, space group P41212, with
a = 65.65 Å, c = 122.04 Å. It confirms the presence of this benzoate ion in spite of the
mutation into a serine of the Cys 47 residue to which the benzoate ion was directly linked
in the wild-type structure. The benzoate ion seems to be stabilized by hydrophobic contacts
on both sides of the aromatic ring. In this matter, the α5 helix, which is specific to peroxiredoxin
5 among mammalian peroxiredoxins, plays an important role. These hydrophobic
contacts also allow to suggest why the benzoate ion disappears when the molecule is
oxidized.
http://hdl.handle.net/2268/57221
http://www.springerlink.com
The original publication is available at www.springerlink.com

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