5k1g: Difference between revisions
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<StructureSection load='5k1g' size='340' side='right'caption='[[5k1g]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5k1g' size='340' side='right'caption='[[5k1g]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5k1g]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5k1g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_vulnificus_MO6-24/O Vibrio vulnificus MO6-24/O]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K1G 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]] 1.899Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5k1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k1g OCA], [https://pdbe.org/5k1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k1g RCSB], [https://www.ebi.ac.uk/pdbsum/5k1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k1g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1Z0YU25_VIBVM A0A1Z0YU25_VIBVM] 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.[RuleBase:RU366011] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Peroxiredoxin|Peroxiredoxin]] | *[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Vibrio vulnificus MO6-24/O]] | ||
[[Category: Ahn | [[Category: Ahn J]] | ||
[[Category: Ha | [[Category: Ha N-C]] | ||
Latest revision as of 22:17, 20 September 2023
Crystal structure of reduced Prx3 from Vibrio vulnificusCrystal structure of reduced Prx3 from Vibrio vulnificus
Structural highlights
FunctionA0A1Z0YU25_VIBVM 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.[RuleBase:RU366011] Publication Abstract from PubMedPeroxiredoxins (Prxs) are ubiquitous cysteine-based peroxidase enzymes. Recently, a new type of Prx, VvPrx3, was identified in the pathogenic bacterium Vibrio vulnificus as being important for survival in macrophages. It employs only one catalytic cysteine residue to decompose peroxides. Here, crystal structures of VvPrx3 representing its reduced and oxidized states have been determined, together with an H2O2-bound structure, at high resolution. The crystal structure representing the reduced Prx3 showed a typical dimeric interface, called the A-type interface. However, VvPrx3 forms an oligomeric interface mediated by a disulfide bond between two catalytic cysteine residues from two adjacent dimers, which differs from the doughnut-like oligomers that appear in most Prxs. Subsequent biochemical studies showed that this disulfide bond was induced by treatment with nitric oxide (NO) as well as with peroxides. Consistently, NO treatment induced expression of the prx3 gene in V. vulnificus, and VvPrx3 was crucial for the survival of bacteria in the presence of NO. Taken together, the function and mechanism of VvPrx3 in scavenging peroxides and NO stress via oligomerization are proposed. These findings contribute to the understanding of the diverse functions of Prxs during pathogenic processes at the molecular level. Crystal structure of peroxiredoxin 3 from Vibrio vulnificus and its implications for scavenging peroxides and nitric oxide.,Ahn J, Jang KK, Jo I, Nurhasni H, Lim JG, Yoo JW, Choi SH, Ha NC IUCrJ. 2018 Jan 1;5(Pt 1):82-92. doi: 10.1107/S205225251701750X. eCollection 2018, Jan 1. PMID:29354274[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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