3o2p: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3o2p]] is a 2 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=3O2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O2P FirstGlance]. <br> | <table><tr><td colspan='2'>[[3o2p]] is a 2 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=3O2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O2P FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o2u|3o2u]], [[3o6b|3o6b]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o2u|3o2u]], [[3o6b|3o6b]]</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]), CDC53, YDL132W, D2190 ([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]), CDC53, YDL132W, D2190 ([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=3o2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o2p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o2p RCSB], [http://www.ebi.ac.uk/pdbsum/3o2p 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=3o2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o2p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o2p RCSB], [http://www.ebi.ac.uk/pdbsum/3o2p 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/CDC53_YEAST CDC53_YEAST]] Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The SCF complex associates with CDC34 as the E2 ubiquitin-conjugating enzyme. The functional specificity of the SCF complex depends on the type of F-box protein. SCF(CDC4) controls the G1-to-S phase transition; it directs ubiquitination of the phosphorylated CDK inhibitor SIC1 and of CDC6. SCF(CDC4) directs ubiquitination of GCN4. SCF(GRR1) directs ubiquitination of phosphorylated CLN1, CLN2 and GIC2. SCF(MET30) directs ubiquitination of MET4. SCF(DIA2) is specifically involved in the pheromone induced degradation of phosphorylated TEC1. SCF(MDM30) seems to direct ubiquitination of FZ01. Involved in the regulation of methionine biosynthesis genes.<ref>PMID:7813440</ref> <ref>PMID:9346238</ref> <ref>PMID:9346239</ref> <ref>PMID:9312054</ref> <ref>PMID:9736614</ref> <ref>PMID:9499404</ref> <ref>PMID:10213692</ref> <ref>PMID:16421250</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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A dual E3 mechanism for Rub1 ligation to Cdc53.,Scott DC, Monda JK, Grace CR, Duda DM, Kriwacki RW, Kurz T, Schulman BA Mol Cell. 2010 Sep 10;39(5):784-96. PMID:20832729<ref>PMID:20832729</ref> | A dual E3 mechanism for Rub1 ligation to Cdc53.,Scott DC, Monda JK, Grace CR, Duda DM, Kriwacki RW, Kurz T, Schulman BA Mol Cell. 2010 Sep 10;39(5):784-96. PMID:20832729<ref>PMID:20832729</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Duda, D M | [[Category: Duda, D M]] | ||
[[Category: Grace, C R.R | [[Category: Grace, C R.R]] | ||
[[Category: Kriwacki, R W | [[Category: Kriwacki, R W]] | ||
[[Category: Kurz, T | [[Category: Kurz, T]] | ||
[[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: Cell cycle]] | [[Category: Cell cycle]] | ||
[[Category: Ligase]] | [[Category: Ligase]] | ||