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| | <StructureSection load='5b6m' size='340' side='right'caption='[[5b6m]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5b6m' size='340' side='right'caption='[[5b6m]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b6m]] is a 6 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=5B6M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B6M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b6m]] is a 6 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=5B6M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B6M FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b6n|5b6n]]</td></tr> | + | </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=5b6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b6m OCA], [https://pdbe.org/5b6m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b6m RCSB], [https://www.ebi.ac.uk/pdbsum/5b6m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b6m ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRDX6, AOP2, KIAA0106 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5b6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b6m OCA], [http://pdbe.org/5b6m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b6m RCSB], [http://www.ebi.ac.uk/pdbsum/5b6m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b6m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRDX6_HUMAN PRDX6_HUMAN]] Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. | + | [https://www.uniprot.org/uniprot/PRDX6_HUMAN PRDX6_HUMAN] Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peroxiredoxin]]
| + | [[Category: Kim EE]] |
| - | [[Category: Kim, E E]] | + | [[Category: Kim KH]] |
| - | [[Category: Kim, K H]] | + | [[Category: Lee WT]] |
| - | [[Category: Lee, W T]] | + | |
| - | [[Category: 1-cys prx]]
| + | |
| - | [[Category: Catalytic site]]
| + | |
| - | [[Category: Oxidation]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Prx6]]
| + | |
| - | [[Category: Reduction]]
| + | |
| Structural highlights
Function
PRDX6_HUMAN Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.
Publication Abstract from PubMed
Peroxiredoxins (Prxs) are a family of antioxidant enzymes found ubiquitously. Prxs function not only as H2O2 scavengers but also as highly sensitive H2O2 sensors and signal transducers. Since reactive oxygen species are involved in many cellular metabolic and signaling processes, Prxs play important roles in various diseases. Prxs can be hyperoxidized to the sulfinic acid (SO2H) or sulfonic acid (SO3H) forms in the presence of high concentrations of H2O2. It is known that oligomerization of Prx is changed accompanying oxidation states, and linked to the function. Among the six Prxs in mammals, Prx6 is the only 1-Cys Prx. It is found in all organs in humans, unlike some 2-Cys Prxs, and is present in all species from bacteria to humans. In addition, Prx6 has Ca2+-independent phospholipase A2 (PLA2) activity. Thus far only the crystal structure of Prx in the oxidized state has been reported. In this study, we present the crystal structures of human Prx6 in the reduced (SH) and the sulfinic acid (SO2H) forms.
Crystal structures of human peroxiredoxin 6 in different oxidation states.,Kim KH, Lee W, Kim EE Biochem Biophys Res Commun. 2016 Jun 25. pii: S0006-291X(16)31052-X. doi:, 10.1016/j.bbrc.2016.06.125. PMID:27353378[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kim KH, Lee W, Kim EE. Crystal structures of human peroxiredoxin 6 in different oxidation states. Biochem Biophys Res Commun. 2016 Jun 25. pii: S0006-291X(16)31052-X. doi:, 10.1016/j.bbrc.2016.06.125. PMID:27353378 doi:http://dx.doi.org/10.1016/j.bbrc.2016.06.125
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