3o2u: Difference between revisions
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==S. cerevisiae Ubc12== | ==S. cerevisiae Ubc12== | ||
<StructureSection load='3o2u' size='340' side='right' caption='[[3o2u]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3o2u' size='340' side='right'caption='[[3o2u]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3o2u]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3o2u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O2U FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.003Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o2u OCA], [https://pdbe.org/3o2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o2u RCSB], [https://www.ebi.ac.uk/pdbsum/3o2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o2u ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o2/3o2u_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o2/3o2u_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 30: | Line 29: | ||
</div> | </div> | ||
<div class="pdbe-citations 3o2u" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3o2u" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Duda | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Grace | [[Category: Duda DM]] | ||
[[Category: Kriwacki | [[Category: Grace CRR]] | ||
[[Category: Kurz | [[Category: Kriwacki RW]] | ||
[[Category: Monda | [[Category: Kurz T]] | ||
[[Category: Schulman | [[Category: Monda JK]] | ||
[[Category: Scott | [[Category: Schulman BA]] | ||
[[Category: Scott DC]] | |||
Latest revision as of 12:26, 6 September 2023
S. cerevisiae Ubc12S. cerevisiae Ubc12
Structural highlights
FunctionUBC12_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.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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