View source for 3tdu


==N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-acetylated Ubc12N complex==
<StructureSection load='3tdu' size='340' side='right'caption='[[3tdu]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3tdu]] is a 6 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=3TDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TDU 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=3tdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tdu OCA], [https://pdbe.org/3tdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tdu RCSB], [https://www.ebi.ac.uk/pdbsum/3tdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tdu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DCNL1_HUMAN DCNL1_HUMAN] Part of an E3 ubiquitin ligase complex for neddylation. Required for neddylation of cullin components of E3 cullin-RING ubiquitin ligase complexes by enhancing the rate of cullins neddylation. Functions to recruit the NEDD8-charged E2 enzyme to the cullin component. Involved in the release of inhibitory effets of CAND1 on cullin-RING ligase E3 complex assembly and activity. Acts also as an oncogene facilitating malignant transformation and carcinogenic progression (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Although most eukaryotic proteins are N-terminally acetylated, structural mechanisms by which N-terminal acetylation mediates protein interactions are largely unknown. Here, we found that N-terminal acetylation of the E2 enzyme, Ubc12, dictates distinctive E3-dependent ligation of the ubiquitin-like protein, Nedd8, to Cul1. Structural, biochemical, biophysical, and genetic analyses revealed how complete burial of Ubc12's N-acetyl-methionine in a hydrophobic pocket in the E3, Dcn1, promotes cullin neddylation. The results suggest that the N-terminal acetyl both directs Ubc12's interactions with Dcn1, and prevents repulsion of a charged N-terminus. Our data provide a link between acetylation and ubiquitin-like protein conjugation, and define a mechanism for N-terminal acetylation-dependent recognition.

N-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein Complex.,Scott DC, Monda JK, Bennett EJ, Harper JW, Schulman BA Science. 2011 Sep 22. PMID:21940857<ref>PMID:21940857</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3tdu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cullin 3D structures|Cullin 3D structures]]
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bennett EJ]]
[[Category: Harper JW]]
[[Category: Monda JK]]
[[Category: Schulman BA]]
[[Category: Scott DC]]