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3tdi
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tdi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TDI FirstGlance]. <br> | <table><tr><td colspan='2'>[[3tdi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TDI FirstGlance]. <br> | ||
| - | </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> | + | </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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tdu|3tdu]], [[3tdz|3tdz]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tdu|3tdu]], [[3tdz|3tdz]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCN1, YLR128W, L3111 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), L2142.3, UBC12, YLR306W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCN1, YLR128W, L3111 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), L2142.3, UBC12, YLR306W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> |
| - | <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=3tdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tdi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tdi RCSB], [http://www.ebi.ac.uk/pdbsum/3tdi PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tdi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tdi RCSB], [http://www.ebi.ac.uk/pdbsum/3tdi PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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> [[http://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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> | 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 | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Bennett, E J | + | [[Category: Bennett, E J]] |
| - | [[Category: Harper, J W | + | [[Category: Harper, J W]] |
| - | [[Category: Monda, J K | + | [[Category: Monda, J K]] |
| - | [[Category: Schulman, B A | + | [[Category: Schulman, B A]] |
| - | [[Category: Scott, D C | + | [[Category: Scott, D C]] |
[[Category: E2:e3]] | [[Category: E2:e3]] | ||
[[Category: Ligase-protein binding complex]] | [[Category: Ligase-protein binding complex]] | ||
Revision as of 22:16, 24 December 2014
yeast Cul1WHB-Dcn1P acetylated Ubc12N complex
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