PDBsum entry 4dss

Oxidoreductase/transport protein

PDB id: 4dss

Contents

Protein chains

174 a.a.

104 a.a.

Waters ×78

PDB id:

4dss

Name:

Oxidoreductase/transport protein

Title:

Crystal structure of peroxiredoxin ahp1 from saccharomyces cerevisiae in complex with thioredoxin trx2

Structure:

Peroxiredoxin type-2. Chain: a. Synonym: ahpc1, cytoplasmic thiol peroxidase 3, ctpx 3, peroxiredoxin type ii, peroxisomal alkyl hydroperoxide reductase, tpx type ii, thiol-specific antioxidant ii, tsa ii, thioredoxin peroxidase type ii, thioredoxin reductase type ii. Engineered: yes. Mutation: yes. Thioredoxin-2.

Source:

Saccharomyces cerevisiae. Yeast. Organism_taxid: 559292. Strain: s288c. Gene: ahp1, l2916, l9354.5, ylr109w. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: g7746, trx1, trx2, ygr209c.

Resolution:

2.10Å R-factor: 0.221 R-free: 0.259

Authors:

F.M.Lian,J.Yu,X.X.Ma,X.J.Yu,Y.Chen,C.Z.Zhou

Key ref:

F.M.Lian et al. (2012). Structural snapshots of yeast alkyl hydroperoxide reductase Ahp1 peroxiredoxin reveal a novel two-cysteine mechanism of electron transfer to eliminate reactive oxygen species. J Biol Chem, 287, 17077-17087. PubMed id: 22474296

Date:

19-Feb-12 Release date: 11-Apr-12

Protein chain

P38013  (AHP1_YEAST) -  Peroxiredoxin AHP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 176 a.a.

Struc: 174 a.a.*

Protein chain

P22803  (TRX2_YEAST) -  Thioredoxin-2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 104 a.a.

Struc: 104 a.a.*

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

Enzyme reactions

• Enzyme class: Chain A: 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

J Biol Chem 287:17077-17087 (2012)

PubMed id: 22474296

Structural snapshots of yeast alkyl hydroperoxide reductase Ahp1 peroxiredoxin reveal a novel two-cysteine mechanism of electron transfer to eliminate reactive oxygen species.

F.M.Lian, J.Yu, X.X.Ma, X.J.Yu, Y.Chen, C.Z.Zhou.

ABSTRACT

No abstract given.