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| | <StructureSection load='6ky4' size='340' side='right'caption='[[6ky4]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='6ky4' size='340' side='right'caption='[[6ky4]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ky4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KY4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KY4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ky4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KY4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 3.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SRX, At1g31170, F28K20.12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sulfiredoxin Sulfiredoxin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.98.2 1.8.98.2] </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=6ky4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ky4 OCA], [https://pdbe.org/6ky4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ky4 RCSB], [https://www.ebi.ac.uk/pdbsum/6ky4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ky4 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=6ky4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ky4 OCA], [http://pdbe.org/6ky4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ky4 RCSB], [http://www.ebi.ac.uk/pdbsum/6ky4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ky4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SRX_ARATH SRX_ARATH]] Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in a peroxiredoxin. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase. Required to switch on the antioxidant pathway to regenerate the oxidative damage. In mitochondrion, catalyzes the retroreduction of the inactive sulfinic form of atypical Prx IIF using thioredoxin as reducing agent.<ref>PMID:17217469</ref> <ref>PMID:20176891</ref> | + | [https://www.uniprot.org/uniprot/SRX_ARATH SRX_ARATH] Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in a peroxiredoxin. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase. Required to switch on the antioxidant pathway to regenerate the oxidative damage. In mitochondrion, catalyzes the retroreduction of the inactive sulfinic form of atypical Prx IIF using thioredoxin as reducing agent.<ref>PMID:17217469</ref> <ref>PMID:20176891</ref> |
| | <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: Arath]] | |
| - | [[Category: Large Structures]] | |
| - | [[Category: Sulfiredoxin]] | |
| - | [[Category: Li, M]] | |
| - | [[Category: Li, X]] | |
| - | [[Category: Liu, M]] | |
| - | [[Category: Sylvanno, M J]] | |
| - | [[Category: Wang, J]] | |
| - | [[Category: Wang, M]] | |
| - | [[Category: Zhang, M]] | |
| - | [[Category: Antioxidant]] | |
| | [[Category: Arabidopsis thaliana]] | | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Cysteine]] | + | [[Category: Large Structures]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Li M]] |
| - | [[Category: Peroxiredoxin repair protein]] | + | [[Category: Li X]] |
| - | [[Category: Sulfinic acid]] | + | [[Category: Liu M]] |
| | + | [[Category: Sylvanno MJ]] |
| | + | [[Category: Wang J]] |
| | + | [[Category: Wang M]] |
| | + | [[Category: Zhang M]] |
| Structural highlights
Function
SRX_ARATH Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in a peroxiredoxin. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase. Required to switch on the antioxidant pathway to regenerate the oxidative damage. In mitochondrion, catalyzes the retroreduction of the inactive sulfinic form of atypical Prx IIF using thioredoxin as reducing agent.[1] [2]
Publication Abstract from PubMed
Typical 2-cysteine peroxiredoxins (2-Cys Prxs) are critical peroxidase sensors and could be deactivated by the hyperoxidation under oxidative stress. In plants, 2-Cys Prxs present at a high level in chloroplasts and are repaired by Sulfiredoxin. Whereas many studies have explored the mechanism of Sulfiredoxin from Homo sapiens (HsSrx), the molecular mechanism of Sulfiredoxin in plants with unique photosynthesis remains unclear. Here we report the crystal structure of Sulfiredoxin from Arabidopsis thaliana (AtSrx), which displayed a typical ParB/Srx fold with an ATP bound at a conservative nucleotide binding motif GCHR. Both the ADP binding pocket and the putative AtSrx-AtPrxA interaction surface of AtSrx are more positively charged comparing to HsSrx, suggesting a robust mechanism of AtSrx. These features illustrate the unique mechanisms of AtSrx, which are vital for figure out the strategies of plants to cope with oxidation stress.
The crystal structure of sulfiredoxin from Arabidopsis thaliana revealed a more robust antioxidant mechanism in plants.,Liu M, Wang J, Li X, Sylvanno MJ, Li M, Zhang M, Wang M Biochem Biophys Res Commun. 2019 Oct 8. pii: S0006-291X(19)31923-0. doi:, 10.1016/j.bbrc.2019.10.034. PMID:31604522[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rey P, Becuwe N, Barrault MB, Rumeau D, Havaux M, Biteau B, Toledano MB. The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response. Plant J. 2007 Feb;49(3):505-14. doi: 10.1111/j.1365-313X.2006.02969.x. Epub 2007 , Jan 1. PMID:17217469 doi:http://dx.doi.org/10.1111/j.1365-313X.2006.02969.x
- ↑ Iglesias-Baena I, Barranco-Medina S, Lazaro-Payo A, Lopez-Jaramillo FJ, Sevilla F, Lazaro JJ. Characterization of plant sulfiredoxin and role of sulphinic form of 2-Cys peroxiredoxin. J Exp Bot. 2010 Mar;61(5):1509-21. doi: 10.1093/jxb/erq016. Epub 2010 Feb 22. PMID:20176891 doi:http://dx.doi.org/10.1093/jxb/erq016
- ↑ Liu M, Wang J, Li X, Sylvanno MJ, Li M, Zhang M, Wang M. The crystal structure of sulfiredoxin from Arabidopsis thaliana revealed a more robust antioxidant mechanism in plants. Biochem Biophys Res Commun. 2019 Oct 8. pii: S0006-291X(19)31923-0. doi:, 10.1016/j.bbrc.2019.10.034. PMID:31604522 doi:http://dx.doi.org/10.1016/j.bbrc.2019.10.034
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