6khx: Difference between revisions
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<StructureSection load='6khx' size='340' side='right'caption='[[6khx]], [[Resolution|resolution]] 2.58Å' scene=''> | <StructureSection load='6khx' size='340' side='right'caption='[[6khx]], [[Resolution|resolution]] 2.58Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6khx]] is a 10 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6khx]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Akkermansia_muciniphila Akkermansia muciniphila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KHX 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]] 2.58Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=6khx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6khx OCA], [https://pdbe.org/6khx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6khx RCSB], [https://www.ebi.ac.uk/pdbsum/6khx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6khx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2N8HPY4_9BACT A0A2N8HPY4_9BACT] | |||
<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 6khx" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6khx" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Akkermansia muciniphila]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Li | [[Category: Li M]] | ||
[[Category: Wang | [[Category: Wang J]] | ||
[[Category: Wang | [[Category: Wang M]] | ||
[[Category: Wang | [[Category: Wang Y]] | ||
[[Category: Xu | [[Category: Xu W]] | ||
[[Category: Zhang | [[Category: Zhang M]] | ||
Latest revision as of 13:33, 22 November 2023
Crystal structure of Prx from Akkermansia muciniphilaCrystal structure of Prx from Akkermansia muciniphila
Structural highlights
FunctionPublication Abstract from PubMedPeroxiredoxins (Prxs) are thiol-specific antioxidant proteins commonly found in organisms that protect cells from the damage of reactive oxygen species produced by metabolism and that participate in cell signaling. The Prx from the bacterium Akkermansia muciniphila (AmPrx) is a typical 2-Cys Prx characterized by two conserved cysteines: Cys49 and Cys183. Here, we verified the peroxidase activity of AmPrx and determined its crystal structure in reduced form, which is a doughnut-shaped decamer composed of five dimers. Particularly, a distinct loop between the alpha4 helix and beta6 strand is involved in the decameric interaction. Deletion of this loop destroys the decameric structure and significantly decreases the peroxidase activity of AmPrx. Our findingss reveal a novel regulatory mechanism of typical 2-Cys Prx, in which the alpha4-beta6 loop affects the assembly of Prx and, therefore, regulates its peroxidase activity. Crystal structure of Akkermansia muciniphila peroxiredoxin reveals a novel regulatory mechanism of typical 2-Cys Prxs by a distinct loop.,Li M, Wang J, Xu W, Wang Y, Zhang M, Wang M FEBS Lett. 2020 Feb 6. doi: 10.1002/1873-3468.13753. PMID:32027024[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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