Peroxiredoxin: Difference between revisions

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<StructureSection load='1qq2' size='350' side='right' scene='43/433646/Cv/2' caption='Typical 2-cys peroxiredoxin dimer complex with Cl- ions [[1qq2]]'>
<StructureSection load='1qq2' size='350' side='right' scene='43/433646/Cv/2' caption='Typical 2-cys peroxiredoxin dimer complex with Cl- ions [[1qq2]]'>
== Function ==
== 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.  
[[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. '''Prx Q''' is the plant homolog of [[Bacterioferritin comigratory protein]].


'''Typical 2-Cys Prx'''<br />
'''Typical 2-Cys Prx'''<br />
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</StructureSection>
</StructureSection>
== 3D Structures of Peroxiredoxin ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*Peroxiredoxin
**[[1qmv]] - h2Cys-Prx – human<br />
**[[1qq2]] – r2Cys-Prx – rat<br />
**[[2a4v]] – yPrx dot5 C-terminal (mutant) – yeast<br />
**[[3cmi]] – yPrx hyr1 - yeast<br />
**[[5ept]] - yPrx tsa2<br />
**[[3sbc]] – yPrx tsa1 (mutant)<br />
**[[5dvb]] - yPrx tsa2 (mutant)<br />
**[[4g2e]] – Prx – ''Sulfolobus tokodaii''<br />
**[[6q5v]] – Prx – ''Sulfolobus islandicus''<br />
**[[5xbr]] – PhPrx – ''Pyrococcus horikoshii''<br />
**[[5xbq]] – PhPrx (mutant) <br />
**[[4llr]] - 2Cys-Prx – ''Trypanosoma cruzi''<br />
**[[1we0]] – Prx – ''Amphibacillus xylanus''<br />
**[[2cv4]], [[2cx3]], [[2cx4]] – ApPrx – ''Aeropyrum pernix''<br />
**[[5xbs]] – ApPrx (mutant) <br />
**[[3drn]] – SsPrx – ''Sulfolobus solfataricus''<br />
**[[3hjp]] – SsPrx (mutant)<br />
**[[3ixr]] – Prx PRXQ (mutant) – ''Xylella fastidiosa''<br />
**[[5epf]] - Prx – ''Mycobacterium tuberculosis''<br />
**[[2c0d]] – Pf2Cys-Prx – ''Plasmodium falciparum''<br />
**[[1xiy]] – Pf1Cys-Prx<br />
**[[1xcc]], [[2h01]], [[3tb2]] - 1Cys-Prx – ''Plasmodium yoelii''<br />
**[[2i81]] - 2Cys-Prx – ''Plasmodium vivax''<br />
**[[6itz]] - TkPrx – ''Thermococcus kodakarensis''<br />
**[[6iu0]], [[6iu1]] – TkPrx (mutant) <br />
**[[6e0f]], [[6e0g]] – 2Cys-Prx – ''Leishmania infantum''<br />
**[[5zte]] – 2Cys-Prx (mutant) – ''Arabidopsis thaliana''<br />
**[[5ovq]] - Prx – ''Aquifex aeolicus''<br />
*Peroxiredoxin 1
**[[4xcs]] - hPrx 1 (mutant) <br />
**[[2rii]], [[3hy2]] – hPrx 1 (mutant)+sulfiredoxin 1<br />
**[[2z9s]] – rPrx 1 (mutant) <br />
**[[3zl5]] - mPrx 1 (mutant) – mouse<br />
**[[5ykj]] – y1Cys-Prx<br />
**[[4kw6]], [[4fh8]] – Prx 1 – ''Ancylostoma ceylanicum''<br />
*Peroxiredoxin 2
**[[5ijt]] – hPrx II <br />
**[[2pwj]] – Prx II – garden pea<br />
**[[4dsq]], [[4dsr]], [[4h86]], [[4owy]] – yPrx II<br />
**[[4dss]] – yPrx II (mutant) + thioredoxin II<br />
**[[1tp9]] – Prx  II – ''Populus trichocarpa''<br />
*Peroxiredoxin 3
**[[1zye]] – Prx III (mutant) – bovine<br />
**[[5ykw]] - yPrx III (mutant) + peptide<br />
**[[5k1g]], [[5k2i]] - VvPrx III (mutant) – ''Vibrio vulnificus''<br />
**[[5k2j]] - VvPrx III (mutant) + H2O2<br />
*Peroxiredoxin 4
**[[3tjf]], [[3tjg]], [[3tjj]], [[3tjk]], [[3tkr]] - hPrx 4 (mutant)<br />
**[[5hqp]] - hPrx 4 (mutant) + ERP44<br />
**[[4rqx]] – hPrx 4 + thioethanesulfonic acid<br />
**[[2pn8]], [[3tjb]], [[3tkp]], [[3tkq]], [[3tks]]  – hPrx 4<br />
**[[3vwu]], [[3vwv]] - mPrx 4 (mutant) <br />
**[[3qpm]] – Prx 4 – ''Larimichtys crocea''<br />
*Peroxiredoxin 5
**[[1urm]] – hPrx 5 (mutant) – human<br />
**[[2vl2]], [[2vl3]], [[2vl9]], [[1h4o]], [[1hd2]], [[1oc3]]  – hPrx 5<br />
**[[3mng]] – hPrx 5+DTT<br />
**[[4k7i]], [[4k7n]], [[4k7o]], [[4mmm]] – hPrx 5 catalytic domain + fragment<br />
**[[2wfc]] – lPrx 5 - lugworm<br />
**[[2xhf]] – Prx 5 – ''Alvinella pompejana''<br />
*Peroxiredoxin 6
**[[5b6m]], [[5b6n]] - hPrx 6<br />
**[[2v2g]] – lPrx 6 <br />
**[[2v32]], [[2v41]] – lPrx 6 (mutant)<br />
*Peroxiredoxin Asp F3
**[[5j9b]] – NfPrx – ''Neosartorya fumigata''<br />
**[[5j9c]] - NfPrx (mutant) <br />


}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 11:27, 2 October 2020

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. Prx Q is the plant homolog of Bacterioferritin comigratory protein.

Typical 2-Cys Prx

  • Prx 1 interacts with signaling molecules[1].
  • Prx 2 is essential for sustaining erythrocyte life span[2].
  • Prx 3 is mitochondria-specific.[3].
  • Prx 4 localizes to the cytoplasm and regulates the activation of NF-κB[4].

Atypical 2-Cys Prx

  • Prx 5 protects from mitochondrial DNA damage induced by H2O2[5].

1-Cys Prx

  • Prx 6 reduces peroxidized membrane phospholipids[6].

Relevance

Prx are over expressed in cancer tissue[7]. Prx 4 mediates osteoclast activation in cancer cells[8].

Structural highlights

In the typical 2-cysteine Prx the [9]. . Water molecules is shown as red sphere.

3D Structures of Peroxiredoxin

Peroxiredoxin 3D structures


Typical 2-cys peroxiredoxin dimer complex with Cl- ions 1qq2

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Neumann CA, Cao J, Manevich Y. Peroxiredoxin 1 and its role in cell signaling. Cell Cycle. 2009 Dec 15;8(24):4072-8. Epub 2009 Dec 5. PMID:19923889 doi:http://dx.doi.org/10.4161/cc.8.24.10242
  2. ↑ Low FM, Hampton MB, Winterbourn CC. Peroxiredoxin 2 and peroxide metabolism in the erythrocyte. Antioxid Redox Signal. 2008 Sep;10(9):1621-30. doi: 10.1089/ars.2008.2081. PMID:18479207 doi:http://dx.doi.org/10.1089/ars.2008.2081
  3. ↑ Chang TS, Cho CS, Park S, Yu S, Kang SW, Rhee SG. Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria. J Biol Chem. 2004 Oct 1;279(40):41975-84. Epub 2004 Jul 27. PMID:15280382 doi:http://dx.doi.org/10.1074/jbc.M407707200
  4. ↑ Fujii J, Ikeda Y, Kurahashi T, Homma T. Physiological and pathological views of peroxiredoxin 4. Free Radic Biol Med. 2015 Jun;83:373-9. doi: 10.1016/j.freeradbiomed.2015.01.025., Epub 2015 Feb 2. PMID:25656995 doi:http://dx.doi.org/10.1016/j.freeradbiomed.2015.01.025
  5. ↑ Banmeyer I, Marchand C, Clippe A, Knoops B. Human mitochondrial peroxiredoxin 5 protects from mitochondrial DNA damages induced by hydrogen peroxide. FEBS Lett. 2005 Apr 25;579(11):2327-33. PMID:15848167 doi:http://dx.doi.org/10.1016/j.febslet.2005.03.027
  6. ↑ Fisher AB. Peroxiredoxin 6: a bifunctional enzyme with glutathione peroxidase and phospholipase A(2) activities. Antioxid Redox Signal. 2011 Aug 1;15(3):831-44. doi: 10.1089/ars.2010.3412. Epub , 2011 Mar 31. PMID:20919932 doi:http://dx.doi.org/10.1089/ars.2010.3412
  7. ↑ Noh DY, Ahn SJ, Lee RA, Kim SW, Park IA, Chae HZ. Overexpression of peroxiredoxin in human breast cancer. Anticancer Res. 2001 May-Jun;21(3B):2085-90. PMID:11497302
  8. ↑ Rafiei S, Tiedemann K, Tabaries S, Siegel PM, Komarova SV. Peroxiredoxin 4: a novel secreted mediator of cancer induced osteoclastogenesis. Cancer Lett. 2015 Jun 1;361(2):262-70. doi: 10.1016/j.canlet.2015.03.012. Epub, 2015 Mar 14. PMID:25779674 doi:http://dx.doi.org/10.1016/j.canlet.2015.03.012
  9. ↑ Hirotsu S, Abe Y, Okada K, Nagahara N, Hori H, Nishino T, Hakoshima T. Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12333-8. PMID:10535922

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