Peroxiredoxin: Difference between revisions

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[[Image:1qq2.png|left|200px|thumb|Crystal Structure of Peroxiredoxin ([[1qq2]])]]
<StructureSection load='1qq2' size='350' side='right' scene='43/433646/Cv/2' caption='Typical 2-cys peroxiredoxin dimer complex with Cl- ions [[1qq2]]'>
{{STRUCTURE_1qq2|  PDB=1qq2  | SIZE=300| SCENE=Peroxiredoxin/Cv/1 |right|CAPTION=Peroxiredoxin [[1qq2]]}}
== 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]].


[[Peroxiredoxin]] (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid byperoxide. The Prxs are divided into typical 2-Cys Prx, atypical 2-Cys Prx and 1-Cys Prx. Prx 5 is expressed in mammalian tissue. The images at the left and at the right correspond to one representative Prx, ''i.e.'' the crystal structure of Peroxiredoxin from rat ([[1qq2]]).
'''Typical 2-Cys Prx'''<br />
* '''Prx 1''' interacts with signaling molecules<ref>PMID:19923889</ref>.
* '''Prx 2''' is essential for sustaining erythrocyte life span<ref>PMID:18479207</ref>.  
* '''Prx 3''' is mitochondria-specific.<ref>PMID:15280382</ref>.
* '''Prx 4''' localizes to the cytoplasm and regulates the activation of NF-κB<ref>PMID:25656995</ref>.  
'''Atypical 2-Cys Prx'''<br />
* '''Prx 5''' protects from mitochondrial DNA damage induced by H<sub>2</sub>O<sub>2</sub><ref>PMID:15848167</ref>.
'''1-Cys Prx'''<br />
* '''Prx 6''' reduces peroxidized membrane phospholipids<ref>PMID:20919932</ref>.  
 
== Relevance ==
Prx are over expressed in cancer tissue<ref>PMID:11497302</ref>. Prx 4 mediates osteoclast activation in cancer cells<ref>PMID:25779674</ref>.
 
== Structural highlights ==
In the typical 2-cysteine Prx the <scene name='43/433646/Cv/5'>Cys-Cys bond is formed between two subunits</scene><ref>PMID:10535922</ref>. <scene name='43/433646/Cv/6'>Cl coordination site</scene>. Water molecules is shown as red sphere.


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== 3D Structures of Peroxiredoxin ==  
== 3D Structures of Peroxiredoxin ==  
[[Peroxiredoxin 3D structures]]


[[1qq2]] – 2Cys-Prx – rat<br />
</StructureSection>
[[2c0d]] – Pf2Cys-Prx – ''Plasmodium falciparum''<br />
[[1xiy]] – Pf1Cys-Prx<br />
[[1xcc]], [[2h01]] - 1Cys-Prx – ''Plasmodium yoelii''<br />
[[2i81]] - 2Cys-Prx – ''Plasmodium vivax''<br />
[[1qmv]] - h2Cys-Prx – human<br />
[[2rii]], [[3hy2]] – hPrx 1 (mutant)+sulfiredoxin 1<br />
[[2z9s]] – Prx 1 (mutant) - rat<br />
[[2pn8]] – hPrx 4<br />
[[1urm]] – hPrx 5 (mutant) – human<br />
[[2vl2]], [[2vl3]], [[2vl9]], [[1h4o]], [[1hd2]], [[1oc3]]  – hPrx 5<br />
[[3mng]] – hPrx 5+DTT<br />
[[2wfc]] – lPrx 5 - lugworm<br />
[[2v2g]] – lPrx 6 <br />
[[2v32]], [[2v41]] – lPrx 6 (mutant)<br />
[[2a4v]] – yPrx dot5 C-termianl (mutant) – yeast<br />
[[3cmi]] – yPrx hyr1<br />
[[1tp9]] – Prx  II – ''Populus trichocarpa''<br />
[[2pwj]] – Prx II – garden pea<br />
[[1uul]] - 2Cys-Prx – ''Trypanosoma cruzi''<br />
[[1we0]] – Prx – ''Amphibacillus xylanus''<br />
[[1zye]] – Prx III (mutant) – bovine<br />
[[2cv4]], [[2cx3]], [[2cx4]] – Prx – ''Aeropyrum pernix''<br />
[[3drn]] – SsPrx – ''Sulfolobus solfataricus''<br />
[[3hjp]] – SsPrx (mutant)<br />
[[3ixr]] – Prx PRXQ (mutant) – ''Xylella fastidiosa''<br />
 


== 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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