22id: Difference between revisions

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'''Unreleased structure'''


The entry 22id is ON HOLD  until Paper Publication
==Structure of Chaetomium thermophilum Ufd1 UT3 domain fused with a ubiquitin C-terminal peptide==
<StructureSection load='22id' size='340' side='right'caption='[[22id]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[22id]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=22ID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=22ID FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14&#8491;</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=22id FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=22id OCA], [https://pdbe.org/22id PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=22id RCSB], [https://www.ebi.ac.uk/pdbsum/22id PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=22id ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G0RYC4_THET3 G0RYC4_THET3]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Cdc48 ATPase (p97 or VCP in mammals) cooperates with its cofactors Ufd1 and Npl4 to extract polyubiquitinated proteins from membranes or multisubunit complexes, promoting their proteasomal degradation. A ubiquitin molecule in the chain is unfolded in an ATP-independent manner and initiates substrate translocation through the central pore of the ATPase. How ubiquitin is unfolded remains unclear. Here we demonstrate that the UT3 domain of Ufd1 specifically interacts with two K48-linked ubiquitins and unfolds one of the ubiquitins by binding its C-terminal beta-strand into a conserved hydrophobic cleft. Simultaneous binding of UT3 to two ubiquitin molecules is required to overcome the energy barrier of ubiquitin unfolding. Subsequently, the UT3-unfolded ubiquitin is captured by Npl4 and Cdc48/p97. Experiments in vitro and in cells show that unfolding-defective mutants of Ufd1 indeed compromise Cdc48/p97 function. Our results provide a reasonable explanation of how simple protein-protein interactions cause the unfolding of the remarkably stable ubiquitin.


Authors:  
ATP-independent unfolding of ubiquitin by Ufd1 initiates Cdc48/p97-mediated substrate processing.,Wang Y, Zhang Z, He W, Wang P, Du J, Pan J, Feng S, Huang J, Ji Z Nat Struct Mol Biol. 2026 Sep 10. doi: 10.1038/s41594-026-01884-7. PMID:42722750<ref>PMID:42722750</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 22id" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
[[Category: Large Structures]]
[[Category: Ji Z]]
[[Category: Wang Y]]
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