View source for 5o71


==Crystal structure of human USP25==
<StructureSection load='5o71' size='340' side='right'caption='[[5o71]], [[Resolution|resolution]] 3.28&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5o71]] is a 1 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=5O71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O71 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]] 3.283&#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=5o71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o71 OCA], [https://pdbe.org/5o71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o71 RCSB], [https://www.ebi.ac.uk/pdbsum/5o71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o71 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UBP25_HUMAN UBP25_HUMAN] Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains.  The muscle-specific isoform (USP25m) may have a role in the regulation of muscular differentiation and function.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
USP25 deubiquitinating enzyme is a key member of the ubiquitin system, which acts as a positive regulator of the Wnt/beta-catenin signaling by promoting the deubiquitination and stabilization of tankyrases. USP25 is characterized by the presence of a long insertion in the middle of the conserved catalytic domain. The crystal structure of USP25 displays an unexpected homotetrameric quaternary assembly that is directly involved in the inhibition of its enzymatic activity. The tetramer is assembled by the association of two dimers and includes contacts between the coiled-coil insertion domain and the ubiquitin-binding pocket at the catalytic domain, revealing a distinctive autoinhibitory mechanism. Biochemical and kinetic assays with dimer, tetramer and truncation constructs of USP25 support this mechanism, displaying higher catalytic activity in the dimer assembly. Moreover, the high stabilization of tankyrases in cultured cells by ectopic expression of a constitutive dimer of USP25 supports a biological relevance of this tetramerization/inhibition mechanism.

A quaternary tetramer assembly inhibits the deubiquitinating activity of USP25.,Liu B, Sureda-Gomez M, Zhen Y, Amador V, Reverter D Nat Commun. 2018 Nov 26;9(1):4973. doi: 10.1038/s41467-018-07510-5. PMID:30478318<ref>PMID:30478318</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5o71" style="background-color:#fffaf0;"></div>

==See Also==
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Liu B]]
[[Category: Reverter D]]