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| | ==Crystal structure of oxidized chimeric EcAhpC1-186-YFSKHN== | | ==Crystal structure of oxidized chimeric EcAhpC1-186-YFSKHN== |
| - | <StructureSection load='5b8a' size='340' side='right' caption='[[5b8a]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='5b8a' size='340' side='right'caption='[[5b8a]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b8a]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B8A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b8a]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B8A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b8b|5b8b]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5b8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b8a OCA], [https://pdbe.org/5b8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b8a RCSB], [https://www.ebi.ac.uk/pdbsum/5b8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b8a ProSAT]</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=5b8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b8a OCA], [http://pdbe.org/5b8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b8a RCSB], [http://www.ebi.ac.uk/pdbsum/5b8a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b8a ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AHPC_ECOLI AHPC_ECOLI]] Directly reduces organic hydroperoxides in its reduced dithiol form. | + | [https://www.uniprot.org/uniprot/AHPC_ECOLI AHPC_ECOLI] Directly reduces organic hydroperoxides in its reduced dithiol form.[https://www.uniprot.org/uniprot/PRDX2_HUMAN PRDX2_HUMAN] Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). |
| | <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: Peroxiredoxin]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Eisenhaber, B]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Eisenhaber, F]] | + | [[Category: Large Structures]] |
| - | [[Category: Gruber, G]] | + | [[Category: Eisenhaber B]] |
| - | [[Category: Kamariah, N]] | + | [[Category: Eisenhaber F]] |
| - | [[Category: Sek, M F]]
| + | [[Category: Gruber G]] |
| - | [[Category: Ahpc]] | + | [[Category: Kamariah N]] |
| - | [[Category: Alkylhydroperoxide reductase]] | + | [[Category: Sek MF]] |
| - | [[Category: Chimeric]] | + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
AHPC_ECOLI Directly reduces organic hydroperoxides in its reduced dithiol form.PRDX2_HUMAN Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2).
Publication Abstract from PubMed
In addition to their antioxidant function, the eukaryotic peroxiredoxins (Prxs) facilitate peroxide-mediated signaling by undergoing controlled inactivation by peroxide-driven over-oxidation. In general, the bacterial enzyme lacks this controlled inactivation mechanism, making it more resistant to high H2O2 concentrations. During peroxide reduction, the active site alternates between reduced, fully folded (FF), and oxidized, locally unfolded (LU) conformations. Here we present novel insights into the divergence of bacterial and human Prxs in robustness and sensitivity to inactivation, respectively. Structural details provide new insights into sub-steps during the catalysis of peroxide reduction, enabling the transition from an FF to a LU conformation. Complementary to mutational and enzymatic results, these data unravel the essential role of the C-terminal tail of bacterial Prxs to act as a molecular switch, mediating the transition from an FF to a LU state. In addition, we propose that the C-terminal tail has influence on the propensity of the disulphide bond formation, indicating that as a consequence on the robustness and sensitivity to over-oxidation. Finally, a physical linkage between the catalytic site, the C-terminal tail and the oligomer interface is described.
Transition steps in peroxide reduction and a molecular switch for peroxide robustness of prokaryotic peroxiredoxins.,Kamariah N, Sek MF, Eisenhaber B, Eisenhaber F, Gruber G Sci Rep. 2016 Nov 28;6:37610. doi: 10.1038/srep37610. PMID:27892488[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kamariah N, Sek MF, Eisenhaber B, Eisenhaber F, Gruber G. Transition steps in peroxide reduction and a molecular switch for peroxide robustness of prokaryotic peroxiredoxins. Sci Rep. 2016 Nov 28;6:37610. doi: 10.1038/srep37610. PMID:27892488 doi:http://dx.doi.org/10.1038/srep37610
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