View source for 7ktx


==Cryo-EM structure of Saccharomyces cerevisiae ER membrane protein complex bound to a Fab in DDM detergent==
<StructureSection load='7ktx' size='340' side='right'caption='[[7ktx]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ktx]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_BY4743 Saccharomyces cerevisiae BY4743]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KTX 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]] 4.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=7ktx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ktx OCA], [https://pdbe.org/7ktx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ktx RCSB], [https://www.ebi.ac.uk/pdbsum/7ktx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ktx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EMC1_YEAST EMC1_YEAST] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Membrane protein biogenesis in the endoplasmic reticulum (ER) is complex and failure-prone. The ER membrane protein complex (EMC), comprising eight conserved subunits, has emerged as a central player in this process. Yet, we have limited understanding of how EMC enables insertion and integrity of diverse clients, from tail-anchored to polytopic transmembrane proteins. Here, yeast and human EMC cryo-EM structures reveal conserved intricate assemblies and human-specific features associated with pathologies. Structure-based functional studies distinguish between two separable EMC activities, as an insertase regulating tail-anchored protein levels and a broader role in polytopic membrane protein biogenesis. These depend on mechanistically coupled yet spatially distinct regions including two lipid-accessible membrane cavities which confer client-specific regulation, and a non-insertase EMC function mediated by the EMC lumenal domain. Our studies illuminate the structural and mechanistic basis of EMC's multifunctionality and point to its role in differentially regulating the biogenesis of distinct client protein classes.

Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients.,Miller-Vedam LE, Brauning B, Popova KD, Schirle Oakdale NT, Bonnar JL, Prabu JR, Boydston EA, Sevillano N, Shurtleff MJ, Stroud RM, Craik CS, Schulman BA, Frost A, Weissman JS Elife. 2020 Nov 25;9. pii: 62611. doi: 10.7554/eLife.62611. PMID:33236988<ref>PMID:33236988</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ktx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae BY4743]]
[[Category: Bonnar JL]]
[[Category: Boydston EA]]
[[Category: Braeuning B]]
[[Category: Craik CS]]
[[Category: Frost A]]
[[Category: Miller-Vedam LE]]
[[Category: Popova KD]]
[[Category: Prabu JR]]
[[Category: Schirle Oakdale NS]]
[[Category: Schulman BA]]
[[Category: Sevillano N]]
[[Category: Shurtleff MJ]]
[[Category: Stroud RM]]
[[Category: Weissman JS]]