Peroxiredoxin: Difference between revisions
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== Structural highlights == | == 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. | 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. | ||
== 3D Structures of Peroxiredoxin == | |||
[[Peroxiredoxin 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
== 3D Structures of Peroxiredoxin == | == 3D Structures of Peroxiredoxin == | ||
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*Peroxiredoxin | *Peroxiredoxin | ||
**[[1qmv]] - h2Cys-Prx – human<br /> | |||
**[[1qq2]] – r2Cys-Prx – rat<br /> | **[[1qq2]] – r2Cys-Prx – rat<br /> | ||
**[[2a4v]] – yPrx dot5 C-terminal (mutant) – yeast<br /> | **[[2a4v]] – yPrx dot5 C-terminal (mutant) – yeast<br /> | ||
**[[3cmi]] – yPrx hyr1 - yeast<br /> | **[[3cmi]] – yPrx hyr1 - yeast<br /> | ||
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**[[3ixr]] – Prx PRXQ (mutant) – ''Xylella fastidiosa''<br /> | **[[3ixr]] – Prx PRXQ (mutant) – ''Xylella fastidiosa''<br /> | ||
**[[5epf]] - Prx – ''Mycobacterium tuberculosis''<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 | *Peroxiredoxin 1 | ||
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**[[2rii]], [[3hy2]] – hPrx 1 (mutant)+sulfiredoxin 1<br /> | **[[2rii]], [[3hy2]] – hPrx 1 (mutant)+sulfiredoxin 1<br /> | ||
**[[2z9s]] – rPrx 1 (mutant) <br /> | **[[2z9s]] – rPrx 1 (mutant) <br /> | ||
**[[3zl5]] - mPrx 1 (mutant) – mouse<br /> | |||
**[[5ykj]] – y1Cys-Prx<br /> | |||
**[[4kw6]], [[4fh8]] – Prx 1 – ''Ancylostoma ceylanicum''<br /> | **[[4kw6]], [[4fh8]] – Prx 1 – ''Ancylostoma ceylanicum''<br /> | ||
*Peroxiredoxin 2 | *Peroxiredoxin 2 | ||
**[[ | **[[5ijt]] – hPrx II <br /> | ||
**[[2pwj]] – Prx II – garden pea<br /> | **[[2pwj]] – Prx II – garden pea<br /> | ||
**[[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 /> | ||
**[[ | **[[1tp9]] – Prx II – ''Populus trichocarpa''<br /> | ||
*Peroxiredoxin 3 | *Peroxiredoxin 3 | ||
**[[1zye]] – Prx III (mutant) – bovine<br /> | **[[1zye]] – Prx III (mutant) – bovine<br /> | ||
**[[5ykw]] - yPrx III (mutant) + peptide<br /> | |||
**[[5k1g]], [[5k2i]] - VvPrx III (mutant) – ''Vibrio vulnificus''<br /> | **[[5k1g]], [[5k2i]] - VvPrx III (mutant) – ''Vibrio vulnificus''<br /> | ||
**[[5k2j]] - VvPrx III (mutant) + H2O2<br /> | **[[5k2j]] - VvPrx III (mutant) + H2O2<br /> | ||
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**[[5hqp]] - hPrx 4 (mutant) + ERP44<br /> | **[[5hqp]] - hPrx 4 (mutant) + ERP44<br /> | ||
**[[4rqx]] – hPrx 4 + thioethanesulfonic acid<br /> | **[[4rqx]] – hPrx 4 + thioethanesulfonic acid<br /> | ||
**[[2pn8]], [[3tjb]], [[3tkp]], [[3tkq]], [[3tks]] – hPrx 4<br /> | **[[2pn8]], [[3tjb]], [[3tkp]], [[3tkq]], [[3tks]] – hPrx 4<br /> | ||
**[[3vwu]], [[3vwv]] - mPrx 4 (mutant) <br /> | **[[3vwu]], [[3vwv]] - mPrx 4 (mutant) <br /> | ||
**[[3qpm]] – Prx 4 – ''Larimichtys crocea''<br /> | |||
*Peroxiredoxin 5 | *Peroxiredoxin 5 | ||
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*Peroxiredoxin 6 | *Peroxiredoxin 6 | ||
**[[5b6m]], [[5b6n]] - hPrx 6<br /> | |||
**[[2v2g]] – lPrx 6 <br /> | **[[2v2g]] – lPrx 6 <br /> | ||
**[[2v32]], [[2v41]] – lPrx 6 (mutant)<br /> | **[[2v32]], [[2v41]] – lPrx 6 (mutant)<br /> | ||
*Peroxiredoxin Asp F3 | *Peroxiredoxin Asp F3 | ||
Revision as of 13:38, 14 November 2019
FunctionPeroxiredoxin (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
Atypical 2-Cys Prx
1-Cys Prx
RelevancePrx are over expressed in cancer tissue[7]. Prx 4 mediates osteoclast activation in cancer cells[8]. Structural highlightsIn the typical 2-cysteine Prx the [9]. . Water molecules is shown as red sphere. 3D Structures of Peroxiredoxin
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3D Structures of Peroxiredoxin3D Structures of Peroxiredoxin
Updated on 14-November-2019
ReferencesReferences
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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:http://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