View source for 4eoz


==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]] 2.40&Aring;' 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]] 2.4&#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=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&reg;/PubMed&reg;, 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]]