4eoz: Difference between revisions
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New page: '''Unreleased structure''' The entry 4eoz is ON HOLD Authors: Prive, G.G., Errington, W.J. Description: Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal doma... |
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==Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain== | |||
<StructureSection load='4eoz' size='340' side='right'caption='[[4eoz]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4eoz]] is a 4 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=4EOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EOZ 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]] 2.4Å</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=4eoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eoz OCA], [https://pdbe.org/4eoz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eoz RCSB], [https://www.ebi.ac.uk/pdbsum/4eoz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eoz ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The E3 ligases recruit substrate proteins for targeted ubiquitylation. Recent insights into the mechanisms of ubiquitylation demonstrate that E3 ligases can possess active regulatory properties beyond those of a simple assembly scaffold. Here, we describe the dimeric structure of the E3 ligase adaptor protein SPOP (speckle-type POZ protein) in complex with the N-terminal domain of Cul3 at 2.4 A resolution. We find that SPOP forms large oligomers that can form heteromeric species with the closely related paralog SPOPL. In combination, SPOP and SPOPL (SPOP-like) form a molecular rheostat that can fine-tune E3 ubiquitin ligase activity by affecting the oligomeric state of the E3 complex. We propose that adaptor protein self-assembly provides a graded level of regulation of the SPOP/Cul3 E3 ligase toward its multiple protein substrates. | |||
Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase.,Errington WJ, Khan MQ, Bueler SA, Rubinstein JL, Chakrabartty A, Prive GG Structure. 2012 Jul 3;20(7):1141-53. Epub 2012 May 24. PMID:22632832<ref>PMID:22632832</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4eoz" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cullin 3D structures|Cullin 3D structures]] | |||
*[[Speckle-type POZ protein 3D structures|Speckle-type POZ protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Errington WJ]] | |||
[[Category: Prive GG]] | |||
Latest revision as of 02:50, 21 November 2024
Crystal structure of the SPOP BTB domain complexed with the Cul3 N-terminal domain
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