The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins
| Autor: | Bernard Knoops, Jean-Paul Declercq, Aude Smeets, Cécile Marchand, Dominique Linard |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular chemistry.chemical_classification Subfamily Protein Conformation Chemistry Stereochemistry Blotting Western Biophysics Peroxiredoxins Crystallography X-Ray Photochemistry Thioredoxin fold Biochemistry chemistry.chemical_compound Biopolymers Protein structure Oxidoreductase Intramolecular force Humans Sulfenic acid Disulfides Peroxiredoxin Oxidation-Reduction Molecular Biology Cysteine |
| Zdroj: | Archives of Biochemistry and Biophysics. 477:98-104 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/j.abb.2008.04.036 |
| Popis: | Peroxiredoxin 5 (PRDX5) belongs to the PRDX superfamily of thiol-dependent peroxidases able to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. PRDX5 is classified in the atypical 2-Cys subfamily of PRDXs. In this subfamily, the oxidized form of the enzyme is characterized by the presence of an intramolecular disulfide bridge between the peroxidatic and the resolving cysteine residues. We report here three crystal forms in which this intramolecular disulfide bond is indeed observed. The structures are characterized by the expected local unfolding of the peroxidatic loop, but also by the unfolding of the resolving loop. A new type of interface between PRDX molecules is described. The three crystal forms were not oxidized in the same way and the influence of the oxidizing conditions is discussed. |
| Databáze: | OpenAIRE |
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