Peroxiredoxin

spinqualitylabelsall models Typical 2-cys peroxiredoxin dimer complex with Cl- ions 1qq2 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Peroxiredoxin (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid hyper oxide forming a Cys-SOH intermediate. A second Cys residue resolves the intermediate to a protein disulfide bond. The Prxs are divided into 3 types according to their intermediate resolving mechanism: typical 2-Cysteine Prx in which the Cys-Cys bond is formed between two subunits, atypical 2-Cys Prx in which the bond is formed within one subunit and 1-Cysteine Prx which uses a single Cys residue for the catalysis. Typical 2-Cys Prx Prx 1 interacts with signaling molecules. Prx 2 is essential for sustaining erythrocyte life span. Prx 3 is mitochondria-specific.. Prx 4 localizes to the cytoplasm and regulates the activation of NF-κB. Atypical 2-Cys Prx Prx 5 protects from mitochondrial DNA damage induced by H2O2. 1-Cys Prx Prx 6 reduces peroxidized membrane phospholipids. Relevance Prx are over expressed in cancer tissue. Prx 4 mediates osteoclast activation in cancer cells. Structural highlights In the typical 2-cysteine Prx the Cys-Cys bond is formed between two subunits. Cl coordination site.

3D Structures of Peroxiredoxin

Updated on 20-November-2016

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• Peroxiredoxin
  • 1qq2 – r2Cys-Prx – rat
    
  • 2c0d – Pf2Cys-Prx – Plasmodium falciparum
    
  • 1xiy – Pf1Cys-Prx
    
  • 1xcc, 2h01, 3tb2 - 1Cys-Prx – Plasmodium yoelii
    
  • 2i81 - 2Cys-Prx – Plasmodium vivax
    
  • 1qmv - h2Cys-Prx – human
    
  • 2a4v – yPrx dot5 C-terminal (mutant) – yeast
    
  • 3cmi – yPrx hyr1 - yeast
    
  • 4g2e – Prx – Sulfolobus tokodaii
    
  • 3sbc – yPrx Tsa1 (mutant)
    
  • 4llr - 2Cys-Prx – Trypanosoma cruzi
    
  • 1we0 – Prx – Amphibacillus xylanus
    
  • 2cv4, 2cx3, 2cx4 – Prx – Aeropyrum pernix
    
  • 3drn – SsPrx – Sulfolobus solfataricus
    
  • 3hjp – SsPrx (mutant)
    
  • 3ixr – Prx PRXQ (mutant) – Xylella fastidiosa
    
• Peroxiredoxin 1
  • 2rii, 3hy2 – hPrx 1 (mutant)+sulfiredoxin 1
    
  • 2z9s – rPrx 1 (mutant)
    
  • 4kw6, 4fh8 – Prx 1 – Ancylostoma ceylanicum
    
  • 3zl5 - mPrx 1 (mutant) – mouse
    
• Peroxiredoxin 2
  • 1tp9 – Prx II – Populus trichocarpa
    
  • 2pwj – Prx II – garden pea
    
  • 4dsq, 4dsr, 4h86, 4owy – yPrx II
    
  • 4dss – yPrx II (mutant) + thioredoxin II
    
• Peroxiredoxin 3
  • 1zye – Prx III (mutant) – bovine
    
• Peroxiredoxin 4
  • 3tjf, 3tjg, 3tjj, 3tjk, 3tkr - hPrx 4 (mutant)
    
  • 4rqx – hPrx 4 + thioethanesulfonic acid
    
  • 3qpm – Prx 4 – Larimichtys crocea
    
  • 2pn8, 3tjb, 3tkp, 3tkq, 3tks – hPrx 4
    
  • 3vwu, 3vwv - mPrx 4 (mutant)
    
• Peroxiredoxin 5
  • 1urm – hPrx 5 (mutant) – human
    
  • 2vl2, 2vl3, 2vl9, 1h4o, 1hd2, 1oc3 – hPrx 5
    
  • 3mng – hPrx 5+DTT
    
  • 4k7i, 4k7n, 4k7o, 4mmm – hPrx 5 catalytic domain + fragment
    
  • 2wfc – lPrx 5 - lugworm
    
  • 2xhf – Prx 5 – Alvinella pompejana
    
• Peroxiredoxin 6
  • 2v2g – lPrx 6
    
  • 2v32, 2v41 – lPrx 6 (mutant)
    

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Alexander Berchansky, Joel L. Sussman, Michal Harel