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6e0f

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

6e0f, resolution 3.70Å

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Retrieved from "http://52.214.119.220/wiki/index.php/6e0f"

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 <SX load='6e0f' size='340' side='right' viewer='molstar' caption='[[6e0f]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6e0f]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Leiin Leiin]. 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://proteopedia.org/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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mTXNPx, LINJ_23_0050 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5671 LEIIN])</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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
 </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>
-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>
 ==See Also==
 *[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </SX>
 [[Category: Large Structures]]
-[[Category: Leiin]]
+[[Category: Leishmania infantum]]
-[[Category: Borchers, C H]]
+[[Category: Borchers CH]]
-[[Category: Castro, H]]
+[[Category: Castro H]]
-[[Category: Jakob, U]]
+[[Category: Jakob U]]
-[[Category: Makepeace, K A.T]]
+[[Category: Makepeace KAT]]
-[[Category: Poole, L B]]
+[[Category: Poole LB]]
-[[Category: Southworth, D R]]
+[[Category: Southworth DR]]
-[[Category: Teixeira, F]]
+[[Category: Teixeira F]]
-[[Category: Tomas, A M]]
+[[Category: Tomas AM]]
-[[Category: Tse, E]]
+[[Category: Tse E]]
-[[Category: Chaperone]]
-[[Category: Client-binding]]
-[[Category: Heat-shock]]
-[[Category: Holdase]]
-[[Category: Unfolding]]

6e0f

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

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