6y4l
From Proteopedia
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==Crystal structure of human ER membrane protein complex subunits EMC2 and EMC9== | ==Crystal structure of human ER membrane protein complex subunits EMC2 and EMC9== | ||
| - | <StructureSection load='6y4l' size='340' side='right'caption='[[6y4l]]' scene=''> | + | <StructureSection load='6y4l' size='340' side='right'caption='[[6y4l]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y4L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Y4L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6y4l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y4L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Y4L FirstGlance]. <br> |
| - | </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=6y4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y4l OCA], [http://pdbe.org/6y4l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y4l RCSB], [http://www.ebi.ac.uk/pdbsum/6y4l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y4l ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EMC2, KIAA0103, TTC35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), EMC9, C14orf122, FAM158A, CGI-112 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6y4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y4l OCA], [http://pdbe.org/6y4l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y4l RCSB], [http://www.ebi.ac.uk/pdbsum/6y4l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y4l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Approximately 25% of eukaryotic genes code for integral membrane proteins that are assembled at the endoplasmic reticulum. An abundant and widely conserved multi-protein complex termed EMC has been implicated in membrane protein biogenesis, but its mechanism of action is poorly understood. Here, we define the composition and architecture of human EMC using biochemical assays, crystallography of individual subunits, site-specific photocrosslinking, and cryo-EM reconstruction. Our results suggest that EMC's cytosolic domain contains a large, moderately hydrophobic vestibule that can bind a substrate's transmembrane domain (TMD). The cytosolic vestibule leads into a lumenally-sealed, lipid-exposed intramembrane groove large enough to accommodate a single substrate TMD. A gap between the cytosolic vestibule and intramembrane groove provides a potential path for substrate egress from EMC. These findings suggest how EMC facilitates energy-independent membrane insertion of TMDs, explain why only short lumenal domains are translocated by EMC, and constrain models of EMC's proposed chaperone function. | ||
| + | |||
| + | The architecture of EMC reveals a path for membrane protein insertion.,O'Donnell JP, Phillips BP, Yagita Y, Juszkiewicz S, Wagner A, Malinverni D, Keenan RJ, Miller EA, Hegde RS Elife. 2020 May 27;9. pii: 57887. doi: 10.7554/eLife.57887. PMID:32459176<ref>PMID:32459176</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6y4l" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hegde | + | [[Category: Donnell, J P.O]] |
| - | [[Category: | + | [[Category: Hegde, R S]] |
| + | [[Category: Complex]] | ||
| + | [[Category: Insertase]] | ||
| + | [[Category: Protein transport]] | ||
Current revision
Crystal structure of human ER membrane protein complex subunits EMC2 and EMC9
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