6ky4

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of Sulfiredoxin from Arabidopsis thaliana

Structural highlights

6ky4 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6ky4"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6ky4 is ON HOLD  until Paper Publication
+==Crystal structure of Sulfiredoxin from Arabidopsis thaliana==
+<StructureSection load='6ky4' size='340' side='right'caption='[[6ky4]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</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='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>
+</table>
+== Function ==
+[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;">
+== 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.
-Authors:
+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<ref>PMID:31604522</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6ky4" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arabidopsis thaliana]]
+[[Category: Large Structures]]
+[[Category: Li M]]
+[[Category: Li X]]
+[[Category: Liu M]]
+[[Category: Sylvanno MJ]]
+[[Category: Wang J]]
+[[Category: Wang M]]
+[[Category: Zhang M]]

6ky4

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Current revision

Crystal structure of Sulfiredoxin from Arabidopsis thaliana

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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