2VL3

Oxidized and reduced forms of human peroxiredoxin 5

2VL3 の概要

• エントリーDOI: 10.2210/pdb2vl3/pdb
• 関連するPDBエントリー: 1H4O 1HD2 1OC3 1URM 2VL2
• 分子名称: PEROXIREDOXIN-5 (2 entities in total)
• 機能のキーワード: thioredoxin peroxidase, alternative initiation, antioxidant enzyme, redox-active center, cytoplasm, peroxidase, peroxisome, antioxidant, polymorphism, mitochondrion, peroxiredoxin, oxidoreductase, transit peptide, thioredoxin fold
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 54581.55

構造登録者

Smeets, A.,Declercq, J.P. (登録日: 2008-01-08, 公開日: 2008-08-26, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.83 Å)