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==Structure of Human Peroxiredoxin 3 as three stacked rings==
==Structure of Human Peroxiredoxin 3 as three stacked rings==
<StructureSection load='5jcg' size='340' side='right' caption='[[5jcg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='5jcg' size='340' side='right'caption='[[5jcg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5jcg]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JCG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JCG FirstGlance]. <br>
<table><tr><td colspan='2'>[[5jcg]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JCG FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.15 1.11.1.15] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jcg OCA], [http://pdbe.org/5jcg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jcg RCSB], [http://www.ebi.ac.uk/pdbsum/5jcg PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jcg OCA], [https://pdbe.org/5jcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jcg RCSB], [https://www.ebi.ac.uk/pdbsum/5jcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jcg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PRDX3_HUMAN PRDX3_HUMAN]] Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.<ref>PMID:12492477</ref>
[https://www.uniprot.org/uniprot/PRDX3_HUMAN PRDX3_HUMAN] Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.<ref>PMID:12492477</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peroxiredoxins are antioxidant proteins primarily responsible for detoxification of hydroperoxides in cells. On exposure to various cellular stresses, peroxiredoxins can acquire chaperone activity, manifested as quaternary reorganization into a high molecular weight (HMW) form. Acidification, for example, causes dodecameric rings of human peroxiredoxin 3 (HsPrx3) to stack into long helical filaments. In this work, a 4.1-A resolution structure of low-pH-instigated helical filaments was elucidated, showing a locally unfolded active site and partially folded C terminus. A 2.8-A crystal structure of HsPrx3 was determined at pH 8.5 under reducing conditions, wherein dodecameric rings are arranged as a short stack, with symmetry similar to low-pH filaments. In contrast to previous observations, the crystal structure displays both a fully folded active site and ordered C terminus, suggesting that the HsPrx3 HMW form maintains catalytic activity. We propose a new role for the HMW form as a self-chaperoning assembly maintaining HsPrx3 function under stress.
 
Structures of Human Peroxiredoxin 3 Suggest Self-Chaperoning Assembly that Maintains Catalytic State.,Yewdall NA, Venugopal H, Desfosses A, Abrishami V, Yosaatmadja Y, Hampton MB, Gerrard JA, Goldstone DC, Mitra AK, Radjainia M Structure. 2016 May 24. pii: S0969-2126(16)30074-0. doi:, 10.1016/j.str.2016.04.013. PMID:27238969<ref>PMID:27238969</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jcg" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Peroxiredoxin]]
[[Category: Homo sapiens]]
[[Category: Gerrard, J A]]
[[Category: Large Structures]]
[[Category: Goldstone, D C]]
[[Category: Gerrard JA]]
[[Category: Yewdall, N A]]
[[Category: Goldstone DC]]
[[Category: Molecular chaperone]]
[[Category: Yewdall NA]]
[[Category: Oxidoreductase]]
[[Category: Peroxidase]]
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