2mt5
From Proteopedia
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| - | ''' | + | ==Isolated Ring domain== |
| + | <StructureSection load='2mt5' size='340' side='right' caption='[[2mt5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mt5]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MT5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2mt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mt5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mt5 RCSB], [http://www.ebi.ac.uk/pdbsum/2mt5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Polyubiquitination by E2 and E3 enzymes is a predominant mechanism regulating protein function. Some RING E3s, including anaphase-promoting complex/cyclosome (APC), catalyze polyubiquitination by sequential reactions with two different E2s. An initiating E2 ligates ubiquitin to an E3-bound substrate. Another E2 grows a polyubiquitin chain on the ubiquitin-primed substrate through poorly defined mechanisms. Here we show that human APC's RING domain is repurposed for dual functions in polyubiquitination. The canonical RING surface activates an initiating E2-ubiquitin intermediate for substrate modification. However, APC engages and activates its specialized ubiquitin chain-elongating E2 UBE2S in ways that differ from current paradigms. During chain assembly, a distinct APC11 RING surface helps deliver a substrate-linked ubiquitin to accept another ubiquitin from UBE2S. Our data define mechanisms of APC/UBE2S-mediated polyubiquitination, reveal diverse functions of RING E3s and E2s, and provide a framework for understanding distinctive RING E3 features specifying ubiquitin chain elongation. | ||
| - | + | Mechanism of Polyubiquitination by Human Anaphase-Promoting Complex: RING Repurposing for Ubiquitin Chain Assembly.,Brown NG, Watson ER, Weissmann F, Jarvis MA, VanderLinden R, Grace CR, Frye JJ, Qiao R, Dube P, Petzold G, Cho SE, Alsharif O, Bao J, Davidson IF, Zheng JJ, Nourse A, Kurinov I, Peters JM, Stark H, Schulman BA Mol Cell. 2014 Oct 8. pii: S1097-2765(14)00716-3. doi:, 10.1016/j.molcel.2014.09.009. PMID:25306923<ref>PMID:25306923</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Brown, N G.]] | ||
| + | [[Category: Frye, J J.]] | ||
| + | [[Category: Jarvis, M.]] | ||
| + | [[Category: Peters, J.]] | ||
| + | [[Category: Petzold, G.]] | ||
| + | [[Category: Qiao, R.]] | ||
| + | [[Category: Royappa, G.]] | ||
| + | [[Category: Schulman, B.]] | ||
| + | [[Category: Stark, H.]] | ||
| + | [[Category: Vanderlinden, R.]] | ||
| + | [[Category: Watson, E R.]] | ||
| + | [[Category: Weissman, F.]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Ring domain]] | ||
| + | [[Category: Zinc binding domain]] | ||
Revision as of 11:17, 29 October 2014
Isolated Ring domain
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