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==Mitochondrial peroxiredoxin from Leishmania infantum in complex with unfolding client protein after heat stress==
==Mitochondrial peroxiredoxin from Leishmania infantum in complex with unfolding client protein after heat stress==
<StructureSection load='6e0f' size='340' side='right' caption='[[6e0f]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
<SX load='6e0f' size='340' side='right' viewer='molstar' caption='[[6e0f]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6e0f]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E0F FirstGlance]. <br>
<table><tr><td colspan='2'>[[6e0f]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_infantum Leishmania infantum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E0F FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6e0g|6e0g]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0f OCA], [http://pdbe.org/6e0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e0f RCSB], [http://www.ebi.ac.uk/pdbsum/6e0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0f ProSAT]</span></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=6e0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0f OCA], [https://pdbe.org/6e0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e0f RCSB], [https://www.ebi.ac.uk/pdbsum/6e0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0f ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A0A6L0XFC6_LEIIN A0A6L0XFC6_LEIIN] Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.[PIRNR:PIRNR000239]
Many 2-Cys-peroxiredoxins (2-Cys-Prxs) are dual-function proteins, either acting as peroxidases under non-stress conditions or as chaperones during stress. The mechanism by which 2-Cys-Prxs switch functions remains to be defined. Our work focuses on Leishmania infantum mitochondrial 2-Cys-Prx, whose reduced, decameric subpopulation adopts chaperone function during heat shock, an activity that facilitates the transition from insects to warm-blooded host environments. Here, we have solved the cryo-EM structure of mTXNPx in complex with a thermally unfolded client protein, and revealed that the flexible N-termini of mTXNPx form a well-resolved central belt that contacts and encapsulates the unstructured client protein in the center of the decamer ring. In vivo and in vitro cross-linking studies provide further support for these interactions, and demonstrate that mTXNPx decamers undergo temperature-dependent structural rearrangements specifically at the dimer-dimer interfaces. These structural changes appear crucial for exposing chaperone-client binding sites that are buried in the peroxidase-active protein.


Chaperone activation and client binding of a 2-cysteine peroxiredoxin.,Teixeira F, Tse E, Castro H, Makepeace KAT, Meinen BA, Borchers CH, Poole LB, Bardwell JC, Tomas AM, Southworth DR, Jakob U Nat Commun. 2019 Feb 8;10(1):659. doi: 10.1038/s41467-019-08565-8. PMID:30737390<ref>PMID:30737390</ref>
==See Also==
 
*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6e0f" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Borchers, C H]]
[[Category: Large Structures]]
[[Category: Castro, H]]
[[Category: Leishmania infantum]]
[[Category: Jakob, U]]
[[Category: Borchers CH]]
[[Category: Makepeace, K A.T]]
[[Category: Castro H]]
[[Category: Poole, L B]]
[[Category: Jakob U]]
[[Category: Southworth, D R]]
[[Category: Makepeace KAT]]
[[Category: Teixeira, F]]
[[Category: Poole LB]]
[[Category: Tomas, A M]]
[[Category: Southworth DR]]
[[Category: Tse, E]]
[[Category: Teixeira F]]
[[Category: Chaperone]]
[[Category: Tomas AM]]
[[Category: Client-binding]]
[[Category: Tse E]]
[[Category: Heat-shock]]
[[Category: Holdase]]
[[Category: Unfolding]]

Latest revision as of 17:38, 13 March 2024

Mitochondrial peroxiredoxin from Leishmania infantum in complex with unfolding client protein after heat stressMitochondrial peroxiredoxin from Leishmania infantum in complex with unfolding client protein after heat stress

6e0f, resolution 3.70Å

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