5imc: Difference between revisions
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==Xanthomonas campestris Peroxiredoxin Q - Structure F3== | ==Xanthomonas campestris Peroxiredoxin Q - Structure F3== | ||
<StructureSection load='5imc' size='340' side='right' caption='[[5imc]], [[Resolution|resolution]] 1.05Å' scene=''> | <StructureSection load='5imc' size='340' side='right'caption='[[5imc]], [[Resolution|resolution]] 1.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5imc]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5imc]] 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=5IMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IMC FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.05Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=5imc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5imc OCA], [https://pdbe.org/5imc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5imc RCSB], [https://www.ebi.ac.uk/pdbsum/5imc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5imc ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </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> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5imc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5imc" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Bacterioferritin comigratory protein|Bacterioferritin comigratory protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Karplus | [[Category: Xanthomonas campestris pv. campestris str. ATCC 33913]] | ||
[[Category: Nelson | [[Category: Karplus A]] | ||
[[Category: Parsonage | [[Category: Nelson KJ]] | ||
[[Category: Perkins | [[Category: Parsonage D]] | ||
[[Category: Poole | [[Category: Perkins A]] | ||
[[Category: Poole LB]] | |||
Latest revision as of 17:01, 30 August 2023
Xanthomonas campestris Peroxiredoxin Q - Structure F3Xanthomonas campestris Peroxiredoxin Q - Structure F3
Structural highlights
FunctionBCP_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.[1] Publication Abstract from PubMedPeroxiredoxins (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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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