3sbc

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(Difference between revisions)

Revision as of 17:54, 5 August 2016

Crystal structure of Saccharomyces cerevisiae TSA1C47S mutant protein

Structural highlights

3sbc is a 10 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	TPX1, TSA, TSA1, YML028W, ZRG14 (ATCC 18824)
Activity:	Peroxiredoxin, with EC number 1.11.1.15
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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.

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.

References

↑ Tairum CA Jr, de Oliveira MA, Horta BB, Zara FJ, Netto LE. Disulfide biochemistry in 2-cys peroxiredoxin: requirement of Glu50 and Arg146 for the reduction of yeast Tsa1 by thioredoxin. 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 doi:http://dx.doi.org/10.1016/j.jmb.2012.09.008

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3sbc"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Saccharomyces cerevisiae TSA1C47S mutant protein==
 <StructureSection load='3sbc' size='340' side='right' caption='[[3sbc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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>
+<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://pdbe.org/3sbc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sbc RCSB], [http://www.ebi.ac.uk/pdbsum/3sbc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sbc ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3sbc" style="background-color:#fffaf0;"></div>
 ==See Also==

3sbc

From Proteopedia

Revision as of 17:54, 5 August 2016

Crystal structure of Saccharomyces cerevisiae TSA1C47S mutant protein

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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