2VL9

Oxidized form of human peroxiredoxin 5

Summary for 2VL9

• Entry DOI: 10.2210/pdb2vl9/pdb
• Related: 1H4O 1HD2 1OC3 1URM 2VL2 2VL3
• Descriptor: PEROXIREDOXIN-5 (2 entities in total)
• Functional Keywords: thioredoxin peroxidase, alternative initiation, antioxidant enzyme, redox-active center, cytoplasm, peroxidase, peroxisome, antioxidant, polymorphism, mitochondrion, peroxiredoxin, oxidoreductase, transit peptide, thioredoxin fold
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 4
• Total formula weight: 73235.92

Authors

Smeets, A.,Declercq, J.P. (deposition date: 2008-01-11, release date: 2008-08-26, Last modification date: 2024-11-13)

Primary citation

Smeets, A.,Marchand, C.,Linard, D.,Knoops, B.,Declercq, J.P.
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.
Arch.Biochem.Biophys., 477:98-, 2008

PubMed Abstract: 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.

PubMed: 18489898
DOI: 10.1016/J.ABB.2008.04.036

Experimental method

X-RAY DIFFRACTION (2.7 Å)