|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of S78C Human Peroxiredoxin 3 as three stacked rings== | | ==Structure of S78C Human Peroxiredoxin 3 as three stacked rings== |
| - | <StructureSection load='5ucx' size='340' side='right' caption='[[5ucx]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='5ucx' size='340' side='right'caption='[[5ucx]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ucx]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UCX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ucx]] 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=5UCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UCX FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zye|1zye]]</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]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRDX3, AOP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5ucx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ucx OCA], [https://pdbe.org/5ucx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ucx RCSB], [https://www.ebi.ac.uk/pdbsum/5ucx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ucx ProSAT]</span></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>
| + | |
| - | <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=5ucx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ucx OCA], [http://pdbe.org/5ucx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ucx RCSB], [http://www.ebi.ac.uk/pdbsum/5ucx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ucx 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 abundant peroxidase enzymes that are key regulators of the cellular redox environment. A major subgroup of these proteins, the typical 2-Cys peroxiredoxins, can switch between dimers and decameric or dodecameric rings, during the catalytic cycle. The necessity of this change in quaternary structure for function as a peroxidase is not fully understood. In order to explore this, human peroxiredoxin 3 (Prx3) protein was engineered to form both obligate dimers (S75E Prx3) and stabilised dodecameric rings (S78C Prx3), uncoupling structural transformations from the catalytic cycle. The obligate dimer, S75E Prx3, retained catalytic activity towards hydrogen peroxide, albeit significantly lower than the wildtype and S78C proteins, suggesting an evolutionary advantage of having higher order self-assemblies.
| + | |
| - | | + | |
| - | Quaternary structure influences the peroxidase activity of peroxiredoxin 3.,Yewdall NA, Peskin AV, Hampton MB, Goldstone DC, Pearce FG, Gerrard JA Biochem Biophys Res Commun. 2018 Feb 10. pii: S0006-291X(18)30322-X. doi:, 10.1016/j.bbrc.2018.02.093. PMID:29438714<ref>PMID:29438714</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5ucx" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Peroxiredoxin]] | + | [[Category: Large Structures]] |
| - | [[Category: Gerrard, J A]] | + | [[Category: Gerrard JA]] |
| - | [[Category: Goldstone, G C]] | + | [[Category: Goldstone GC]] |
| - | [[Category: Yewdall, N A]] | + | [[Category: Yewdall NA]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxidase]]
| + | |
| - | [[Category: Peroxiredoxin 3]]
| + | |
| - | [[Category: Stacked ring]]
| + | |
| - | [[Category: Typical 2-cy]]
| + | |
