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| <StructureSection load='6ww7' size='340' side='right'caption='[[6ww7]], [[Resolution|resolution]] 3.40Å' scene=''> | | <StructureSection load='6ww7' size='340' side='right'caption='[[6ww7]], [[Resolution|resolution]] 3.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6ww7]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WW7 FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WW7 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></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</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='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=6ww7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ww7 OCA], [https://pdbe.org/6ww7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ww7 RCSB], [https://www.ebi.ac.uk/pdbsum/6ww7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ww7 ProSAT]</span></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=6ww7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ww7 OCA], [https://pdbe.org/6ww7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ww7 RCSB], [https://www.ebi.ac.uk/pdbsum/6ww7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ww7 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Disease ==
| |
| [[https://www.uniprot.org/uniprot/EMC1_HUMAN EMC1_HUMAN]] Global developmental delay-visual anomalies-progressive cerebellar atrophy-truncal hypotonia syndrome. The disease is caused by mutations affecting the gene represented in this entry.
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| == Function ==
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| [[https://www.uniprot.org/uniprot/EMC10_HUMAN EMC10_HUMAN]] Promotes angiogenesis and tissue repair in the heart after myocardial infarction. Stimulates cardiac endothelial cell migration and outgrowth via the activation of p38 MAPK, PAK and MAPK2 signaling pathways.<ref>PMID:28931551</ref> [[https://www.uniprot.org/uniprot/MMGT1_HUMAN MMGT1_HUMAN]] Mediates Mg(2+) transport.[UniProtKB:Q8K273]
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| A defining step in the biogenesis of a membrane protein is the insertion of its hydrophobic transmembrane helices into the lipid bilayer. The nine-subunit ER membrane protein complex (EMC) is a conserved co- and post-translational insertase at the endoplasmic reticulum. We determined the structure of the human EMC in a lipid nanodisc to an overall resolution of 3.4 A by cryo-electron microscopy, permitting building of a nearly complete atomic model. We used structure-guided mutagenesis to demonstrate that substrate insertion requires a methionine-rich cytosolic loop and occurs via an enclosed hydrophilic vestibule within the membrane formed by the subunits EMC3 and EMC6. We propose that the EMC uses local membrane thinning and a positively charged patch to decrease the energetic barrier for insertion into the bilayer.
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| Structural basis for membrane insertion by the human ER membrane protein complex.,Pleiner T, Pinton Tomaleri G, Januszyk K, Inglis AJ, Hazu M, Voorhees RM Science. 2020 May 21. pii: science.abb5008. doi: 10.1126/science.abb5008. PMID:32439656<ref>PMID:32439656</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6ww7" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Homo sapiens]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Inglis, A J]] | | [[Category: Inglis AJ]] |
| [[Category: Januszyk, K]] | | [[Category: Januszyk K]] |
| [[Category: Pleiner, T]] | | [[Category: Pleiner T]] |
| [[Category: Tomaleri, G P]] | | [[Category: Tomaleri GP]] |
| [[Category: Voorhees, R M]] | | [[Category: Voorhees RM]] |
| [[Category: Endoplasmic reticulum]]
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| [[Category: Insertase]]
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| [[Category: Membrane protein]]
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| [[Category: Transmembrane chaperone]]
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