3sbc: Difference between revisions
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==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]] 2.80Å' scene=''> | <StructureSection load='3sbc' size='340' side='right'caption='[[3sbc]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3sbc]] is a 10 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3sbc]] is a 10 chain structure with sequence from [https://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 [https://proteopedia.org/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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPX1, TSA, TSA1, YML028W, ZRG14 ([https://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'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sbc OCA], [https://pdbe.org/3sbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sbc RCSB], [https://www.ebi.ac.uk/pdbsum/3sbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sbc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Peroxiredoxin|Peroxiredoxin]] | *[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | |||
[[Category: Peroxiredoxin]] | [[Category: Peroxiredoxin]] | ||
[[Category: Horta, B B]] | [[Category: Horta, B B]] | ||
Revision as of 10:49, 29 June 2022
Crystal structure of Saccharomyces cerevisiae TSA1C47S mutant proteinCrystal structure of Saccharomyces cerevisiae TSA1C47S mutant protein
Structural highlights
Function[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. Publication Abstract from PubMed2-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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