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| | ==Crystal Structure of S. cerevisiae TSA2 in the disulfide state== | | ==Crystal Structure of S. cerevisiae TSA2 in the disulfide state== |
| - | <StructureSection load='5ept' size='340' side='right' caption='[[5ept]], [[Resolution|resolution]] 5.00Å' scene=''> | + | <StructureSection load='5ept' size='340' side='right'caption='[[5ept]], [[Resolution|resolution]] 5.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ept]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EPT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EPT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ept]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EPT FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dvb|5dvb]]</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]] 5Å</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=5ept FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ept OCA], [https://pdbe.org/5ept PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ept RCSB], [https://www.ebi.ac.uk/pdbsum/5ept PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ept 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=5ept FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ept OCA], [http://pdbe.org/5ept PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ept RCSB], [http://www.ebi.ac.uk/pdbsum/5ept PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TSA2_YEAST TSA2_YEAST]] Reduces peroxides. May play an important role in eliminating peroxides generated during metabolism (By similarity). | + | [https://www.uniprot.org/uniprot/TSA2_YEAST TSA2_YEAST] Reduces peroxides. May play an important role in eliminating peroxides generated during metabolism (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5ept" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5ept" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Peroxiredoxin]] | + | [[Category: Large Structures]] |
| - | [[Category: Jenner, L B]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Kidmose, R T]] | + | [[Category: Jenner LB]] |
| - | [[Category: Nielsen, M H]] | + | [[Category: Kidmose RT]] |
| - | [[Category: Oxidative stress]] | + | [[Category: Nielsen MH]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxidase]]
| + | |
| Structural highlights
Function
TSA2_YEAST Reduces peroxides. May play an important role in eliminating peroxides generated during metabolism (By similarity).
Publication Abstract from PubMed
Saccharomyces cerevisiae TSA2 belongs to the family of typical 2-Cys peroxiredoxins, a ubiquitously expressed family of redox-active enzymes that utilize a conserved peroxidatic cysteine to reduce peroxides. Typical 2-Cys peroxiredoxins have been shown to be involved in protection against oxidative stress and in hydrogen peroxide signalling. Furthermore, several 2-Cys peroxiredoxins, including S. cerevisiae TSA1 and TSA2, are able to switch to chaperone activity upon hyperoxidation of their peroxidatic cysteine. This makes the sensitivity to hyperoxidation of the peroxidatic cysteine a very important determinant for the cellular function of a peroxiredoxin under different cellular conditions. Typical 2-Cys peroxiredoxins exist as dimers, and in the course of the reaction the peroxidatic cysteine forms a disulfide with a resolving cysteine located in the C-terminus of its dimeric partner. This requires a local unfolding of the active site and the C-terminus. The balance between the fully folded and locally unfolded conformations is of key importance for the reactivity and sensitivity to hyperoxidation of the different peroxiredoxins. Here, the structure of a C48S mutant of TSA2 from S. cerevisiae that mimics the reduced state of the peroxidatic cysteine has been determined. The structure reveals a novel conformation for the strictly conserved Pro41, which is likely to affect the delicate balance between the fully folded and locally unfolded conformations of the active site, and therefore the reactivity and the sensitivity to hyperoxidation. Furthermore, the structure also explains the observed difference in the pKa values of the peroxidatic cysteines of S. cerevisiae TSA1 and TSA2 despite their very high sequence identity.
Structure of TSA2 reveals novel features of the active-site loop of peroxiredoxins.,Nielsen MH, Kidmose RT, Jenner LB Acta Crystallogr D Struct Biol. 2016 Jan;72(Pt 1):158-67. doi:, 10.1107/S2059798315023815. Epub 2016 Jan 1. PMID:26894543[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nielsen MH, Kidmose RT, Jenner LB. Structure of TSA2 reveals novel features of the active-site loop of peroxiredoxins. Acta Crystallogr D Struct Biol. 2016 Jan;72(Pt 1):158-67. doi:, 10.1107/S2059798315023815. Epub 2016 Jan 1. PMID:26894543 doi:http://dx.doi.org/10.1107/S2059798315023815
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