8c07: Difference between revisions

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'''Unreleased structure'''


The entry 8c07 is ON HOLD  until Paper Publication
==Structure of HECT E3 UBR5 forming K48 linked Ubiquitin chains==
<StructureSection load='8c07' size='340' side='right'caption='[[8c07]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8c07]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8C07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8C07 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SY8:5-azanylpentan-2-one'>SY8</scene></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=8c07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8c07 OCA], [https://pdbe.org/8c07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8c07 RCSB], [https://www.ebi.ac.uk/pdbsum/8c07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8c07 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ubiquitin (Ub) chain formation by homologous to E6AP C-terminus (HECT)-family E3 ligases regulates vast biology, yet the structural mechanisms remain unknown. We used chemistry and cryo-electron microscopy (cryo-EM) to visualize stable mimics of the intermediates along K48-linked Ub chain formation by the human E3, UBR5. The structural data reveal a approximately 620 kDa UBR5 dimer as the functional unit, comprising a scaffold with flexibly tethered Ub-associated (UBA) domains, and elaborately arranged HECT domains. Chains are forged by a UBA domain capturing an acceptor Ub, with its K48 lured into the active site by numerous interactions between the acceptor Ub, manifold UBR5 elements and the donor Ub. The cryo-EM reconstructions allow defining conserved HECT domain conformations catalyzing Ub transfer from E2 to E3 and from E3. Our data show how a full-length E3, ubiquitins to be adjoined, E2 and intermediary products guide a feed-forward HECT domain conformational cycle establishing a highly efficient, broadly targeting, K48-linked Ub chain forging machine.


Authors:  
Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5.,Hehl LA, Horn-Ghetko D, Prabu JR, Vollrath R, Vu DT, Perez Berrocal DA, Mulder MPC, van der Heden van Noort GJ, Schulman BA Nat Chem Biol. 2024 Feb;20(2):190-200. doi: 10.1038/s41589-023-01414-2. Epub 2023 , Aug 24. PMID:37620400<ref>PMID:37620400</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 8c07" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
*[[3D structures of ubiquitin|3D structures of ubiquitin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Hehl LA]]
[[Category: Prabu JR]]
[[Category: Schulman BA]]
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