5v6p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 5v6p is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (14:10, 13 March 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5v6p is ON HOLD
+
==CryoEM structure of the ERAD-associated E3 ubiquitin-protein ligase HRD1==
 +
<SX load='5v6p' size='340' side='right' viewer='molstar' caption='[[5v6p]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
 +
</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>
-
Authors:
+
==See Also==
-
 
+
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
-
Description:
+
== References ==
-
[[Category: Unreleased Structures]]
+
<references/>
 +
__TOC__
 +
</SX>
 +
[[Category: Large Structures]]
 +
[[Category: Saccharomyces cerevisiae S288C]]
 +
[[Category: Liao M]]
 +
[[Category: Mi W]]
 +
[[Category: Rapoport TA]]
 +
[[Category: Schoebel S]]
 +
[[Category: Stein A]]

Current revision

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

5v6p, resolution 4.10Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5v6p"
Personal tools