6vk1
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CryoEM structure of Hrd1/Hrd3 part from Hrd1-Usa1/Der1/Hrd3 complex== | |
| - | + | <StructureSection load='6vk1' size='340' side='right'caption='[[6vk1]], [[Resolution|resolution]] 3.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6vk1]] 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=6VK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VK1 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9Å</td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vk1 OCA], [https://pdbe.org/6vk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vk1 RCSB], [https://www.ebi.ac.uk/pdbsum/6vk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vk1 ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HRD1_YEAST HRD1_YEAST] E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC1 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome. ERAD-M substrates are processed by the same HRD1-HRD3 core complex, but only a subset of the other components is required for ERAD-M.<ref>PMID:10218484</ref> <ref>PMID:10547371</ref> <ref>PMID:10793145</ref> <ref>PMID:11018054</ref> <ref>PMID:11139575</ref> <ref>PMID:11146622</ref> <ref>PMID:11390656</ref> <ref>PMID:16619026</ref> <ref>PMID:16873066</ref> <ref>PMID:20005842</ref> <ref>PMID:21074049</ref> <ref>PMID:8970163</ref> <ref>PMID:9437001</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Rapoport TA]] | ||
| + | [[Category: Wu X]] | ||
Current revision
CryoEM structure of Hrd1/Hrd3 part from Hrd1-Usa1/Der1/Hrd3 complex
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