3o6b

<StructureSection load='3o6b' size='340' side='right' caption='[[3o6b]], [[Resolution|resolution]] 3.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[3o6b]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O6B FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o2p|3o2p]], [[3o2u|3o2u]]</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 ATCC 18824]), CDC53, YDL132W, D2190 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3o6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o6b OCA], [http://pdbe.org/3o6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o6b RCSB], [http://www.ebi.ac.uk/pdbsum/3o6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o6b ProSAT]</span></td></tr>

[[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>

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== Publication Abstract from PubMed ==

In ubiquitin-like protein (UBL) cascades, a thioester-linked E2 approximately UBL complex typically interacts with an E3 enzyme for UBL transfer to the target. Here we demonstrate a variant mechanism, whereby the E2 Ubc12 functions with two E3s, Hrt1 and Dcn1, for ligation of the UBL Rub1 to Cdc53's WHB subdomain. Hrt1 functions like a conventional RING E3, with its N terminus recruiting Cdc53 and C-terminal RING activating Ubc12 approximately Rub1. Dcn1's "potentiating neddylation" domain (Dcn1(P)) acts as an additional E3, reducing nonspecific Hrt1-mediated Ubc12 approximately Rub1 discharge and directing Ubc12's active site to Cdc53. Crystal structures of Dcn1(P)-Cdc53(WHB) and Ubc12 allow modeling of a catalytic complex, supported by mutational data. We propose that Dcn1's interactions with both Cdc53 and Ubc12 would restrict the otherwise flexible Hrt1 RING-bound Ubc12 approximately Rub1 to a catalytically competent orientation. Our data reveal mechanisms by which two E3s function synergistically to promote UBL transfer from one E2 to a target.

 

<div class="pdbe-citations 3o6b" style="background-color:#fffaf0;"></div>

[[Category: Atcc 18824]]

[[Category: Duda, D M]]

[[Category: Grace, C R.R]]

[[Category: Kriwacki, R W]]

[[Category: Kurz, T]]

[[Category: Monda, J K]]

[[Category: Schulman, B A]]

[[Category: Scott, D C]]

[[Category: Ligase]]