6wb9
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structure of the S. cerevisiae ER membrane complex== | |
+ | <StructureSection load='6wb9' size='340' side='right'caption='[[6wb9]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6wb9]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_w303 Saccharomyces cerevisiae w303]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WB9 FirstGlance]. <br> | ||
+ | </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>, <scene name='pdbligand=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</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=6wb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wb9 OCA], [https://pdbe.org/6wb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wb9 RCSB], [https://www.ebi.ac.uk/pdbsum/6wb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wb9 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[https://www.uniprot.org/uniprot/EMC5_YEAST EMC5_YEAST]] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [[https://www.uniprot.org/uniprot/EMC2_YEAST EMC2_YEAST]] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [[https://www.uniprot.org/uniprot/EMC6_YEAST EMC6_YEAST]] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [[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). [[https://www.uniprot.org/uniprot/SOP4_YEAST SOP4_YEAST]] Involved in the export of PMA1, possibly through the monitoring or assisting of PMA1 folding and acquisition of competence to enter vesicles.<ref>PMID:12230471</ref> <ref>PMID:9265642</ref> [[https://www.uniprot.org/uniprot/EMC10_YEAST EMC10_YEAST]] Non essential component of the endoplasmic reticulum (ER) membrane protein complex (EMC) involved in ER-associated degradation (ERAD) and proper assembly of multi-pass transmembrane proteins (Probable). EMC acts in yeast as an ER-mitochondria tether that interacts with outer membrane protein TOM5 of TOM (translocase of the mitochondrial outer membrane) complex (Probable).<ref>PMID:26512320</ref> [[https://www.uniprot.org/uniprot/EMC3_YEAST EMC3_YEAST]] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [[https://www.uniprot.org/uniprot/EMC4_YEAST EMC4_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 == | ||
+ | The endoplasmic reticulum (ER) membrane complex (EMC) cooperates with the Sec61 translocon to co-translationally insert a transmembrane helix (TMH) of many multi-pass integral membrane proteins into the ER membrane, and it is also responsible for inserting the TMH of some tail-anchored proteins(1-3). How EMC accomplishes this feat has been unclear. Here we report the first, to our knowledge, cryo-electron microscopy structure of the eukaryotic EMC. We found that the Saccharomyces cerevisiae EMC contains eight subunits (Emc1-6, Emc7 and Emc10), has a large lumenal region and a smaller cytosolic region, and has a transmembrane region formed by Emc4, Emc5 and Emc6 plus the transmembrane domains of Emc1 and Emc3. We identified a five-TMH fold centred around Emc3 that resembles the prokaryotic YidC insertase and that delineates a largely hydrophilic client protein pocket. The transmembrane domain of Emc4 tilts away from the main transmembrane region of EMC and is partially mobile. Mutational studies demonstrated that the flexibility of Emc4 and the hydrophilicity of the client pocket are required for EMC function. The EMC structure reveals notable evolutionary conservation with the prokaryotic insertases(4,5), suggests that eukaryotic TMH insertion involves a similar mechanism, and provides a framework for detailed understanding of membrane insertion for numerous eukaryotic integral membrane proteins and tail-anchored proteins. | ||
- | + | Structure of the ER membrane complex, a transmembrane-domain insertase.,Bai L, You Q, Feng X, Kovach A, Li H Nature. 2020 Jun 3. pii: 10.1038/s41586-020-2389-3. doi:, 10.1038/s41586-020-2389-3. PMID:32494008<ref>PMID:32494008</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6wb9" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Saccharomyces cerevisiae w303]] | ||
+ | [[Category: Bai, L]] | ||
+ | [[Category: Li, H]] | ||
+ | [[Category: Complex]] | ||
+ | [[Category: Er]] | ||
+ | [[Category: Insertase]] | ||
+ | [[Category: Membrane protein]] |
Current revision
Structure of the S. cerevisiae ER membrane complex
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