PDBsum entry 2vl2

Oxidoreductase

PDB id: 2vl2

Contents

Protein chain

162 a.a. *

Ligands

BEZ ×2

Waters ×390

* Residue conservation analysis

PDB id:

2vl2

Name:

Oxidoreductase

Title:

Oxidized and reduced forms of human peroxiredoxin 5

Structure:

Peroxiredoxin-5. Chain: a, b. Fragment: residues 2-162. Synonym: prx-v, peroxisomal antioxidant enzyme, plp, thioredoxin reductase, thioredoxin peroxidase pmp20, antioxidant enzyme b166, aoeb166, tpx type vi, liver tissue 2d-page spot 71b, alu corepressor 1, human peroxiredoxin 5. Engineered: yes. Peroxiredoxin-5.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Organ: lung. Expressed in: escherichia coli m15. Expression_system_taxid: 1007065.

Resolution:

1.93Å R-factor: 0.207 R-free: 0.255

Authors:

A.Smeets,J.P.Declercq

Key ref:

A.Smeets et al. (2008). 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. PubMed id: 18489898 DOI: 10.1016/j.abb.2008.04.036

Date:

08-Jan-08 Release date: 26-Aug-08

Protein chains

P30044  (PRDX5_HUMAN) -  Peroxiredoxin-5, mitochondrial from Homo sapiens

Seq: 214 a.a.

Struc: 162 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.1.11.1.24 - thioredoxin-dependent peroxiredoxin.
• Reaction: a hydroperoxide + [thioredoxin]-dithiol = an alcohol + [thioredoxin]- disulfide + H2O

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/j.abb.2008.04.036

Arch Biochem Biophys 477:98 (2008)

PubMed id: 18489898

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.

A.Smeets, C.Marchand, D.Linard, B.Knoops, J.P.Declercq.

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.