6e0f: Difference between revisions
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==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]] 3.70Å' scene=''> | |||
== 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> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6e0g|6e0g]]</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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6e0f" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Borchers, C H]] | |||
[[Category: Castro, H]] | |||
[[Category: Jakob, U]] | |||
[[Category: Makepeace, K A.T]] | |||
[[Category: Poole, L B]] | |||
[[Category: Southworth, D R]] | |||
[[Category: Teixeira, F]] | |||
[[Category: Tomas, A M]] | |||
[[Category: Tse, E]] | |||
[[Category: Chaperone]] | |||
[[Category: Client-binding]] | |||
[[Category: Heat-shock]] | |||
[[Category: Holdase]] | |||
[[Category: Unfolding]] | |||
Revision as of 06:39, 21 February 2019
Mitochondrial peroxiredoxin from Leishmania infantum in complex with unfolding client protein after heat stress
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