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| 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  [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) > >] | |
| 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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