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3tdi
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==yeast Cul1WHB-Dcn1P acetylated Ubc12N complex== | |
| + | <StructureSection load='3tdi' size='340' side='right'caption='[[3tdi]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3tdi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TDI FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tdu|3tdu]], [[3tdz|3tdz]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCN1, YLR128W, L3111 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), L2142.3, UBC12, YLR306W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=3tdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tdi OCA], [https://pdbe.org/3tdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tdi RCSB], [https://www.ebi.ac.uk/pdbsum/3tdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tdi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/DCN1_YEAST DCN1_YEAST]] Required for neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity. Does not act by preventing deneddylation, but rather facilitates neddylation, possibly by acting with HRT1/RBX1 to recruit the Nedd8-charged E2 UBC12 to the cullin component of SCF-type complexes.<ref>PMID:15988528</ref> [[https://www.uniprot.org/uniprot/UBC12_YEAST UBC12_YEAST]] Accepts the ubiquitin-like protein NEDD8/RUB1 from the UBA3-ULA1 E1 complex and catalyzes its covalent attachment to other proteins. The major substrate is CDC53/Cullin.<ref>PMID:9545234</ref> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3tdi" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Baker's yeast]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bennett, E J]] | ||
| + | [[Category: Harper, J W]] | ||
| + | [[Category: Monda, J K]] | ||
| + | [[Category: Schulman, B A]] | ||
| + | [[Category: Scott, D C]] | ||
| + | [[Category: E2:e3]] | ||
| + | [[Category: Ligase-protein binding complex]] | ||
Current revision
yeast Cul1WHB-Dcn1P acetylated Ubc12N complex
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