View source for 5vnz


==Structure of a TRAF6-Ubc13~Ub complex==
<StructureSection load='5vnz' size='340' side='right'caption='[[5vnz]], [[Resolution|resolution]] 3.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vnz]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VNZ 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]] 3.41&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5vnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vnz OCA], [https://pdbe.org/5vnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vnz RCSB], [https://www.ebi.ac.uk/pdbsum/5vnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vnz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRAF6_DANRE TRAF6_DANRE] E3 ubiquitin-protein ligase that mediates ubiquitination of proteins. Adapter protein that seems to play a role in signal transduction.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ubiquitin chains linked through lysine63 (K63) play a critical role in inflammatory signalling. Following ligand engagement of immune receptors, the RING E3 ligase TRAF6 builds K63-linked chains together with the heterodimeric E2 enzyme Ubc13-Uev1A. Dimerisation of the TRAF6 RING domain is essential for the assembly of K63-linked ubiquitin chains. Here, we show that TRAF6 RING dimers form a catalytic complex where one RING interacts with a Ubc13~Ubiquitin conjugate, while the zinc finger 1 (ZF1) domain and linker-helix of the opposing monomer contact ubiquitin. The RING dimer interface is conserved across TRAFs and we also show that TRAF5-TRAF6 heterodimers form. Importantly, TRAF5 can provide ZF1, enabling ubiquitin transfer from a TRAF6-bound Ubc13 conjugate. Our study explains the dependence of activity on TRAF RING dimers, and suggests that both homo- and heterodimers mediated by TRAF RING domains have the capacity to synthesise ubiquitin chains.

The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1.,Middleton AJ, Budhidarmo R, Das A, Zhu J, Foglizzo M, Mace PD, Day CL Nat Commun. 2017 Nov 27;8(1):1788. doi: 10.1038/s41467-017-01665-3. PMID:29176576<ref>PMID:29176576</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vnz" style="background-color:#fffaf0;"></div>

==See Also==
*[[TNF receptor-associated factor 3D structures|TNF receptor-associated factor 3D structures]]
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Danio rerio]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Day CL]]
[[Category: Middleton AJ]]