8gxr
From Proteopedia
(Difference between revisions)
m (Protected "8gxr" [edit=sysop:move=sysop]) |
|||
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==crystal structure of UBC domain of UBE2O== | |
| + | <StructureSection load='8gxr' size='340' side='right'caption='[[8gxr]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8gxr]] is a 4 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=8GXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GXR 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]] 1.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=8gxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gxr OCA], [https://pdbe.org/8gxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gxr RCSB], [https://www.ebi.ac.uk/pdbsum/8gxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gxr 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8gxr" style="background-color:#fffaf0;"></div> |
| - | [[Category: Fu | + | == References == |
| - | [[Category: Zhu | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Trametes pubescens]] | ||
| + | [[Category: Fu Z]] | ||
| + | [[Category: Huang H]] | ||
| + | [[Category: Zhu W]] | ||
Current revision
crystal structure of UBC domain of UBE2O
| |||||||||||
