7un6: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[7un6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UN6 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7un6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7un6 OCA], [https://pdbe.org/7un6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7un6 RCSB], [https://www.ebi.ac.uk/pdbsum/7un6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7un6 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7un6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7un6 OCA], [https://pdbe.org/7un6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7un6 RCSB], [https://www.ebi.ac.uk/pdbsum/7un6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7un6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/UBE2O_HUMAN UBE2O_HUMAN]] E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins (PubMed:23455153, PubMed:24703950). Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity (PubMed:23381138). Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis (PubMed:23455153). Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting their subcellular location (PubMed:24703950). Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASHC1, leading to promote endosomal F-actin assembly (PubMed:23452853).<ref>PMID:23381138</ref> <ref>PMID:23452853</ref> <ref>PMID:23455153</ref> <ref>PMID:24703950</ref>
+[https://www.uniprot.org/uniprot/UBE2O_HUMAN UBE2O_HUMAN] E2/E3 hybrid ubiquitin-protein ligase that displays both E2 and E3 ligase activities and mediates monoubiquitination of target proteins (PubMed:23455153, PubMed:24703950). Negatively regulates TRAF6-mediated NF-kappa-B activation independently of its E2 activity (PubMed:23381138). Acts as a positive regulator of BMP7 signaling by mediating monoubiquitination of SMAD6, thereby regulating adipogenesis (PubMed:23455153). Mediates monoubiquitination at different sites of the nuclear localization signal (NLS) of BAP1, leading to cytoplasmic retention of BAP1. Also able to monoubiquitinate the NLS of other chromatin-associated proteins, such as INO80 and CXXC1, affecting their subcellular location (PubMed:24703950). Acts as a regulator of retrograde transport by assisting the TRIM27:MAGEL2 E3 ubiquitin ligase complex to mediate 'Lys-63'-linked ubiquitination of WASHC1, leading to promote endosomal F-actin assembly (PubMed:23452853).<ref>PMID:23381138</ref> <ref>PMID:23452853</ref> <ref>PMID:23455153</ref> <ref>PMID:24703950</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The E2/E3 enzyme UBE2O ubiquitylates diverse clients to mediate important processes, including targeting unassembled 'orphan' proteins for quality control and clearing ribosomes during erythropoiesis. How quality-control factors, such as UBE2O, select clients on the basis of heterogeneous features is largely unknown. Here, we show that UBE2O client selection is regulated by ubiquitin binding and a cofactor, NAP1L1. Attaching a single ubiquitin onto a client enhances UBE2O binding and multi-mono-ubiquitylation. UBE2O also repurposes the histone chaperone NAP1L1 as an adapter to recruit a subset of clients. Cryo-EM structures of human UBE2O in complex with NAP1L1 reveal a malleable client recruitment interface that is autoinhibited by the intrinsically reactive UBC domain. Adding a ubiquitylated client identifies a distinct ubiquitin-binding SH3-like domain required for client selection. Our findings reveal how multivalency and a feed-forward mechanism drive the selection of protein quality-control clients.
-Mechanism of client selection by the protein quality-control factor UBE2O.,Yip MCJ, Sedor SF, Shao S Nat Struct Mol Biol. 2022 Aug;29(8):774-780. doi: 10.1038/s41594-022-00807-6., Epub 2022 Aug 1. PMID:35915257<ref>PMID:35915257</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7un6" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>