5v6p

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m (Protected "5v6p" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5v6p is ON HOLD
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==CryoEM structure of the ERAD-associated E3 ubiquitin-protein ligase HRD1==
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<SX load='5v6p' size='340' side='right' viewer='molstar' caption='[[5v6p]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5v6p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V6P FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5v6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v6p OCA], [https://pdbe.org/5v6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v6p RCSB], [https://www.ebi.ac.uk/pdbsum/5v6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v6p ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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Authors:
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==See Also==
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
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Description:
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</SX>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Liao M]]
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[[Category: Mi W]]
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[[Category: Rapoport TA]]
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[[Category: Schoebel S]]
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[[Category: Stein A]]

Current revision

CryoEM structure of the ERAD-associated E3 ubiquitin-protein ligase HRD1

5v6p, resolution 4.10Å

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OCA

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