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{{STRUCTURE_3sbc|  PDB=3sbc  |  SCENE=  }}
==Crystal structure of Saccharomyces cerevisiae TSA1C47S mutant protein==
===Crystal structure of Saccharomyces cerevisiae TSA1C47S mutant protein===
<StructureSection load='3sbc' size='340' side='right' caption='[[3sbc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
{{ABSTRACT_PUBMED_22985967}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3sbc]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SBC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=DTV:(2S,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTV</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPX1, TSA, TSA1, YML028W, ZRG14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3sbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sbc RCSB], [http://www.ebi.ac.uk/pdbsum/3sbc PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/TSA1_YEAST TSA1_YEAST]] Physiologically important antioxidant which constitutes an enzymatic defense against sulfur-containing radicals. Can provide protection against a thiol-containing oxidation system but not against an oxidation system without thiol.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
2-Cys peroxiredoxin (Prx) enzymes are ubiquitously distributed peroxidases that make use of a peroxidatic cysteine (Cys(P)) to decompose hydroperoxides. A disulfide bond is generated as a consequence of the partial unfolding of the alpha-helix that contains Cys(P). Therefore, during its catalytic cycle, 2-Cys Prx alternates between two states, locally unfolded and fully folded. Tsa1 (thiol-specific antioxidant protein 1 from yeast) is by far the most abundant Cys-based peroxidase in Saccharomyces cerevisiae. In this work, we present the crystallographic structure at 2.8A resolution of Tsa1(C47S) in the decameric form [(alpha(2))(5)] with a DTT molecule bound to the active site, representing one of the few available reports of a 2-Cys Prx (AhpC-Prx1 subfamily) (AhpC, alkyl hydroperoxide reductase subunit C) structure that incorporates a ligand. The analysis of the Tsa1(C47S) structure indicated that Glu50 and Arg146 participate in the stabilization of the Cys(P) alpha-helix. As a consequence, we raised the hypothesis that Glu50 and Arg146 might be relevant to the Cys(P) reactivity. Therefore, Tsa1(E50A) and Tsa1(R146Q) mutants were generated and were still able to decompose hydrogen peroxide, presenting a second-order rate constant in the range of 10(6)M(-1)s(-1). Remarkably, although Tsa1(E50A) and Tsa1(R146Q) were efficiently reduced by the low-molecular-weight reductant DTT, these mutants displayed only marginal thioredoxin (Trx)-dependent peroxidase activity, indicating that Glu50 and Arg146 are important for the Tsa1-Trx interaction. These results may impact the comprehension of downstream events of signaling pathways that are triggered by the oxidation of critical Cys residues, such as Trx.


==Function==
Disulfide biochemistry in 2-cys peroxiredoxin: requirement of Glu50 and Arg146 for the reduction of yeast Tsa1 by thioredoxin.,Tairum CA Jr, de Oliveira MA, Horta BB, Zara FJ, Netto LE J Mol Biol. 2012 Nov 23;424(1-2):28-41. doi: 10.1016/j.jmb.2012.09.008. Epub 2012, Sep 15. PMID:22985967<ref>PMID:22985967</ref>
[[http://www.uniprot.org/uniprot/TSA1_YEAST TSA1_YEAST]] Physiologically important antioxidant which constitutes an enzymatic defense against sulfur-containing radicals. Can provide protection against a thiol-containing oxidation system but not against an oxidation system without thiol.  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3sbc]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SBC OCA].
</div>


==See Also==
==See Also==
*[[Peroxiredoxin|Peroxiredoxin]]
*[[Peroxiredoxin|Peroxiredoxin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:022985967</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Atcc 18824]]
[[Category: Peroxiredoxin]]
[[Category: Peroxiredoxin]]
[[Category: Horta, B B.]]
[[Category: Horta, B B]]
[[Category: Netto, L E.S.]]
[[Category: Netto, L E.S]]
[[Category: Oliveira, M A.]]
[[Category: Oliveira, M A]]
[[Category: Tairum, C A.]]
[[Category: Tairum, C A]]
[[Category: Alpha-beta fold]]
[[Category: Alpha-beta fold]]
[[Category: Cytosol]]
[[Category: Cytosol]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]
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