Article (Scientific journals)
Crystal structure of the C47S mutant of human peroxiredoxin 5
Evrard, Christine; Smeets, Aude; Knoops, Bernard et al.
2004In Journal of Chemical Crystallography, 34, p. 553-558
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Keywords :
Antioxidant enzyme; peroxiredoxin; thioredoxin fold; thioredoxin peroxidase
Abstract :
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Evrard, Christine ;  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;  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)
Language :
English
Title :
Crystal structure of the C47S mutant of human peroxiredoxin 5
Publication date :
2004
Journal title :
Journal of Chemical Crystallography
ISSN :
1074-1542
eISSN :
1572-8854
Publisher :
Springer Science & Business Media B.V.
Volume :
34
Pages :
553-558
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 27 May 2010

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