View source for 9quf


==Structure of a fungal Ube2O==
<StructureSection load='9quf' size='340' side='right'caption='[[9quf]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9quf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrenophora_tritici-repentis Pyrenophora tritici-repentis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9QUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9QUF 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=9quf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9quf OCA], [https://pdbe.org/9quf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9quf RCSB], [https://www.ebi.ac.uk/pdbsum/9quf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9quf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A922SUA0_9PLEO A0A922SUA0_9PLEO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
UBE2O is a promiscuous ubiquitin ligase involved in cellular quality control pathways. Along with BIRC6, UBE2O is one of only two E2 enzymes that can ubiquitinate substrates in an E3-independent manner. The E2/E3 hybrid targets and multi-monoubiquitinates a multitude of orphan proteins; however, the mechanisms underlying substrate specificity and ubiquitin transfer remain poorly understood. By combining structural and biochemical approaches, we show that substrate binding by UBE2O occurs through a conserved acidic pocket formed by the N-terminal SH3-like domains and that this platform allows the recruitment of a broad range of proteins. Furthermore, we identified specific residues in the catalytic UBC domain that position ubiquitin in a closed state, confirming its confirmation, and priming it for nucleophilic attack by the incoming substrate. Importantly, the activated E2 approximately Ub conjugate is protected by a tryptophan residue, avoiding premature hydrolysis. By incorporating these findings into the UBC domain of BIRC6 our data provide the molecular basis of how specialized E2/E3 hybrid proteins function as potent ubiquitination enzymes reminiscent of the catalytic principle of RING E3 ligases.

Structural basis for substrate recruitment and catalytic ubiquitin transfer by the E2/E3 hybrid enzyme UBE2O.,Kordic D, Williams TL, Deszcz L, Ehrmann JF, Arnese R, Schleiffer A, Clausen T, Meinhart A J Biol Chem. 2025 Dec 17;302(2):111073. doi: 10.1016/j.jbc.2025.111073. PMID:41419192<ref>PMID:41419192</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9quf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrenophora tritici-repentis]]
[[Category: Arnese R]]
[[Category: Clausen T]]
[[Category: Ehrmann J]]
[[Category: Kordic D]]
[[Category: Luiza Deszcz L]]
[[Category: Meinhart A]]
[[Category: Williams TL]]