6vk3

<table><tr><td colspan='2'>[[6vk3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VK3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VK3 FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hrd3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), YOS9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vk3 OCA], [http://pdbe.org/6vk3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vk3 RCSB], [http://www.ebi.ac.uk/pdbsum/6vk3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vk3 ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/OS9_YEAST OS9_YEAST]] Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. The recognition of targets is N-glycan specific.<ref>PMID:12077121</ref> <ref>PMID:15556621</ref> <ref>PMID:16168370</ref> <ref>PMID:16168371</ref> <ref>PMID:16168372</ref>

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== Publication Abstract from PubMed ==

Misfolded luminal endoplasmic reticulum (ER) proteins undergo ER-associated degradation (ERAD-L): They are retrotranslocated into the cytosol, polyubiquitinated, and degraded by the proteasome. ERAD-L is mediated by the Hrd1 complex (composed of Hrd1, Hrd3, Der1, Usa1, and Yos9), but the mechanism of retrotranslocation remains mysterious. Here, we report a structure of the active Hrd1 complex, as determined by cryo-electron microscopy analysis of two subcomplexes. Hrd3 and Yos9 jointly create a luminal binding site that recognizes glycosylated substrates. Hrd1 and the rhomboid-like Der1 protein form two "half-channels" with cytosolic and luminal cavities, respectively, and lateral gates facing one another in a thinned membrane region. These structures, along with crosslinking and molecular dynamics simulation results, suggest how a polypeptide loop of an ERAD-L substrate moves through the ER membrane.

Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex.,Wu X, Siggel M, Ovchinnikov S, Mi W, Svetlov V, Nudler E, Liao M, Hummer G, Rapoport TA Science. 2020 Apr 24;368(6489). pii: 368/6489/eaaz2449. doi:, 10.1126/science.aaz2449. PMID:32327568<ref>PMID:32327568</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Rapoport, T A]]

[[Category: Wu, X]]

[[Category: Ubiquitination]]