7yw1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (19:26, 26 February 2025) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 7yw1 is ON HOLD until Paper Publication
+
==crystal structure of UBE2O==
 +
<StructureSection load='7yw1' size='340' side='right'caption='[[7yw1]], [[Resolution|resolution]] 3.27&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[7yw1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trametes_pubescens Trametes pubescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YW1 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]] 3.27&#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=7yw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yw1 OCA], [https://pdbe.org/7yw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yw1 RCSB], [https://www.ebi.ac.uk/pdbsum/7yw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yw1 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/A0A1M2VY70_TRAPU A0A1M2VY70_TRAPU]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The E2/E3 hybrid enzyme UBE2O plays important roles in key biological events, but its autoubiquitination mechanism remains largely unclear. In this study, we determined the crystal structures of full-length (FL) UBE2O from Trametes pubescens (tp) and its ubiquitin-conjugating (UBC) domain. The dimeric FL-tpUBE2O structure revealed interdomain interactions between the conserved regions (CR1-CR2) and UBC. The dimeric intermolecular and canonical ubiquitin/UBC interactions are mechanistically important for UBE2O functions in catalyzing the formation of free polyubiquitin chains and substrate ubiquitination. Beyond dimerization, autoubiquitination within the CR1-CR2 domain also regulates tpUBE2O activity. Additionally, we show that tpUBE2O catalyzes the formation of all seven types of polyubiquitin chains in vitro. The CR1-CR2/UBC and canonical ubiquitin/UBC interactions are important for the polyubiquitination of AMP-activated protein kinase alpha2 (AMPKalpha2) by human UBE2O (hUBE2O), which leads to tumorigenesis. These structural insights lay the groundwork for understanding UBE2O's mechanisms and developing structure-based therapeutics targeting UBE2O.
-
Authors:
+
Structural insights into the biochemical mechanism of the E2/E3 hybrid enzyme UBE2O.,Huang H, Zhu W, Huang B, Fu Z, Xiong Y, Cao D, Ye Y, Chang Q, Li W, Li L, Zhou H, Niu X, Zhang W Structure. 2025 Feb 6;33(2):274-288.e4. doi: 10.1016/j.str.2024.12.002. Epub 2024 , Dec 30. PMID:39740670<ref>PMID:39740670</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 7yw1" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Trametes pubescens]]
 +
[[Category: Fu Z]]
 +
[[Category: Huang H]]
 +
[[Category: Zhu W]]

Current revision

crystal structure of UBE2O

PDB ID 7yw1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools