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| Line 38: |
Line 38: |
| **[[5dvb]] - yPrx tsa2 (mutant)<br /> | | **[[5dvb]] - yPrx tsa2 (mutant)<br /> |
| **[[4g2e]] – Prx – ''Sulfolobus tokodaii''<br /> | | **[[4g2e]] – Prx – ''Sulfolobus tokodaii''<br /> |
| | **[[6gww]] – Prx – ''Sulfolobus islandicus''<br /> |
| | **[[5xbr]] – PhPrx – ''Pyrococcus horikoshii''<br /> |
| | **[[5xbq]] – PhPrx (mutant) <br /> |
| **[[4llr]] - 2Cys-Prx – ''Trypanosoma cruzi''<br /> | | **[[4llr]] - 2Cys-Prx – ''Trypanosoma cruzi''<br /> |
| **[[1we0]] – Prx – ''Amphibacillus xylanus''<br /> | | **[[1we0]] – Prx – ''Amphibacillus xylanus''<br /> |
| **[[2cv4]], [[2cx3]], [[2cx4]] – Prx – ''Aeropyrum pernix''<br /> | | **[[2cv4]], [[2cx3]], [[2cx4]] – ApPrx – ''Aeropyrum pernix''<br /> |
| | **[[5xbs]] – ApPrx (mutant) <br /> |
| **[[3drn]] – SsPrx – ''Sulfolobus solfataricus''<br /> | | **[[3drn]] – SsPrx – ''Sulfolobus solfataricus''<br /> |
| **[[3hjp]] – SsPrx (mutant)<br /> | | **[[3hjp]] – SsPrx (mutant)<br /> |
| Line 60: |
Line 64: |
| **[[4dsq]], [[4dsr]], [[4h86]], [[4owy]] – yPrx II<br /> | | **[[4dsq]], [[4dsr]], [[4h86]], [[4owy]] – yPrx II<br /> |
| **[[4dss]] – yPrx II (mutant) + thioredoxin II<br /> | | **[[4dss]] – yPrx II (mutant) + thioredoxin II<br /> |
| | **[[5ijt]] – hPrx II <br /> |
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| *Peroxiredoxin 3 | | *Peroxiredoxin 3 |
| 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[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 Cys-Cys bond is formed between two subunits[9]. Cl coordination site.
- ↑ 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:https://dx.doi.org/10.4161/cc.8.24.10242
- ↑ 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:https://dx.doi.org/10.1089/ars.2008.2081
- ↑ 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:https://dx.doi.org/10.1074/jbc.M407707200
- ↑ 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:https://dx.doi.org/10.1016/j.freeradbiomed.2015.01.025
- ↑ 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:https://dx.doi.org/10.1016/j.febslet.2005.03.027
- ↑ 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:https://dx.doi.org/10.1089/ars.2010.3412
- ↑ 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
- ↑ 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:https://dx.doi.org/10.1016/j.canlet.2015.03.012
- ↑ 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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3D Structures of Peroxiredoxin
Updated on 16-August-2018
{"openlevels":0}
- 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
- 5ept - yPrx tsa2
- 3sbc – yPrx tsa1 (mutant)
- 5dvb - yPrx tsa2 (mutant)
- 4g2e – Prx – Sulfolobus tokodaii
- 6gww – Prx – Sulfolobus islandicus
- 5xbr – PhPrx – Pyrococcus horikoshii
- 5xbq – PhPrx (mutant)
- 4llr - 2Cys-Prx – Trypanosoma cruzi
- 1we0 – Prx – Amphibacillus xylanus
- 2cv4, 2cx3, 2cx4 – ApPrx – Aeropyrum pernix
- 5xbs – ApPrx (mutant)
- 3drn – SsPrx – Sulfolobus solfataricus
- 3hjp – SsPrx (mutant)
- 3ixr – Prx PRXQ (mutant) – Xylella fastidiosa
- 5epf - Prx – Mycobacterium tuberculosis
- Peroxiredoxin 1
- 4xcs - hPrx 1 (mutant)
- 2rii, 3hy2 – hPrx 1 (mutant)+sulfiredoxin 1
- 2z9s – rPrx 1 (mutant)
- 4kw6, 4fh8 – Prx 1 – Ancylostoma ceylanicum
- 3zl5 - mPrx 1 (mutant) – mouse
- Peroxiredoxin 2
- Peroxiredoxin 3
- 1zye – Prx III (mutant) – bovine
- 5k1g, 5k2i - VvPrx III (mutant) – Vibrio vulnificus
- 5k2j - VvPrx III (mutant) + H2O2
- Peroxiredoxin 4
- Peroxiredoxin 5
- Peroxiredoxin 6
- Peroxiredoxin Asp F3
- 5j9b – NfPrx – Neosartorya fumigata
- 5j9c - NfPrx (mutant)
References