6e0g

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<SX load='6e0g' size='340' side='right' viewer='molstar' caption='[[6e0g]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<SX load='6e0g' size='340' side='right' viewer='molstar' caption='[[6e0g]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6e0g]] 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=6E0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E0G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6e0g]] 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=6E0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E0G FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6e0f|6e0f]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6e0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0g OCA], [https://pdbe.org/6e0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e0g RCSB], [https://www.ebi.ac.uk/pdbsum/6e0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0g ProSAT]</span></td></tr>
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<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=6e0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e0g OCA], [http://pdbe.org/6e0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e0g RCSB], [http://www.ebi.ac.uk/pdbsum/6e0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e0g ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6e0g" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Leiin]]
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[[Category: Leishmania infantum]]
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[[Category: Borchers, C H]]
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[[Category: Borchers CH]]
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[[Category: Castro, H]]
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[[Category: Castro H]]
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[[Category: Jakob, U]]
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[[Category: Jakob U]]
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[[Category: Makepeace, K A.T]]
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[[Category: Makepeace KAT]]
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[[Category: Poole, L B]]
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[[Category: Poole LB]]
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[[Category: Southworth, D R]]
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[[Category: Southworth DR]]
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[[Category: Teixeira, F]]
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[[Category: Teixeira F]]
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[[Category: Tomas, A M]]
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[[Category: Tomas AM]]
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[[Category: Tse, E]]
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[[Category: Tse E]]
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[[Category: Chaperone]]
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[[Category: Client-binding]]
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[[Category: Heat-shock]]
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[[Category: Holdase]]
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[[Category: Unfolding]]
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Current revision

Mitochondrial peroxiredoxin from Leishmania infantum after heat stress without unfolding client protein

6e0g, resolution 2.90Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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