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3tdu

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==N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-acetylated Ubc12N complex==
==N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-acetylated Ubc12N complex==
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<StructureSection load='3tdu' size='340' side='right' caption='[[3tdu]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='3tdu' size='340' side='right'caption='[[3tdu]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tdu]] is a 6 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TDU FirstGlance]. <br>
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<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>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
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</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>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tdi|3tdi]], [[3tdz|3tdz]]</td></tr>
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<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>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCUN1D1, DCUN1L1, RP42, SCCRO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), CUL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<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>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tdu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tdu RCSB], [http://www.ebi.ac.uk/pdbsum/3tdu PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[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).
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Ubiquitin conjugating enzyme|Ubiquitin conjugating enzyme]]
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*[[Cullin 3D structures|Cullin 3D structures]]
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== References ==
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*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bennett, E J.]]
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[[Category: Large Structures]]
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[[Category: Harper, J W.]]
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[[Category: Bennett EJ]]
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[[Category: Monda, J K.]]
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[[Category: Harper JW]]
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[[Category: Schulman, B A.]]
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[[Category: Monda JK]]
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[[Category: Scott, D C.]]
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[[Category: Schulman BA]]
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[[Category: E2:e3]]
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[[Category: Scott DC]]
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[[Category: Ligase-protein binding complex]]
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Current revision

N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-acetylated Ubc12N complex

PDB ID 3tdu

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