View source for 5iox


==Xanthomonas campestris Peroxiredoxin Q - Structure LUss==
<StructureSection load='5iox' size='340' side='right'caption='[[5iox]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5iox]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris_str._ATCC_33913 Xanthomonas campestris pv. campestris str. ATCC 33913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IOX 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]] 1.3&#8491;</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=5iox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iox OCA], [https://pdbe.org/5iox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iox RCSB], [https://www.ebi.ac.uk/pdbsum/5iox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iox ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BCP_XANCP BCP_XANCP] Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.<ref>PMID:19477183</ref> 
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== Publication Abstract from PubMed ==
Peroxiredoxins (Prxs) are ubiquitous cysteine-based peroxidases that guard cells against oxidative damage, are virulence factors for pathogens, and are involved in eukaryotic redox regulatory pathways. We have analyzed catalytically active crystals to capture atomic resolution snapshots of a PrxQ subfamily enzyme (from Xanthomonas campestris) proceeding through thiolate, sulfenate, and sulfinate species. These analyses provide structures of unprecedented accuracy for seeding theoretical studies, and reveal conformational intermediates giving insight into the reaction pathway. Based on a highly non-standard geometry seen for the sulfenate intermediate, we infer that the sulfenate formation itself can strongly promote local unfolding of the active site to enhance productive catalysis. Further, these structures reveal that preventing local unfolding, in this case via crystal contacts, results in facile hyperoxidative inactivation even for Prxs normally resistant to such inactivation. This supports previous proposals that conformation-specific inhibitors may be useful for achieving selective inhibition of Prxs that are drug targets.

Peroxiredoxin Catalysis at Atomic Resolution.,Perkins A, Parsonage D, Nelson KJ, Ogba OM, Cheong PH, Poole LB, Karplus PA Structure. 2016 Sep 1. pii: S0969-2126(16)30223-4. doi:, 10.1016/j.str.2016.07.012. PMID:27594682<ref>PMID:27594682</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5iox" style="background-color:#fffaf0;"></div>

==See Also==
*[[Bacterioferritin comigratory protein|Bacterioferritin comigratory protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xanthomonas campestris pv. campestris str. ATCC 33913]]
[[Category: Karplus A]]
[[Category: Nelson KJ]]
[[Category: Parsonage D]]
[[Category: Perkins A]]
[[Category: Poole LB]]