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6wb9

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Structure of the S. cerevisiae ER membrane complex

Structural highlights

6wb9 is a 7 chain structure with sequence from Saccharomyces cerevisiae w303. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[EMC5_YEAST] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [EMC2_YEAST] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [EMC6_YEAST] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [EMC1_YEAST] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [SOP4_YEAST] Involved in the export of PMA1, possibly through the monitoring or assisting of PMA1 folding and acquisition of competence to enter vesicles.^[1] ^[2] [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).^[3] [EMC3_YEAST] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [EMC4_YEAST] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER).

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Luo WJ, Gong XH, Chang A. An ER membrane protein, Sop4, facilitates ER export of the yeast plasma membrane [H+]ATPase, Pma1. Traffic. 2002 Oct;3(10):730-9. doi: 10.1034/j.1600-0854.2002.31005.x. PMID:12230471 doi:http://dx.doi.org/10.1034/j.1600-0854.2002.31005.x
↑ Luo W, Chang A. Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant. J Cell Biol. 1997 Aug 25;138(4):731-46. PMID:9265642
↑ Wideman JG. The ubiquitous and ancient ER membrane protein complex (EMC): tether or not? F1000Res. 2015 Aug 25;4:624. doi: 10.12688/f1000research.6944.2. eCollection, 2015. PMID:26512320 doi:http://dx.doi.org/10.12688/f1000research.6944.2
↑ Bai L, You Q, Feng X, Kovach A, Li H. Structure of the ER membrane complex, a transmembrane-domain insertase. Nature. 2020 Jun 3. pii: 10.1038/s41586-020-2389-3. doi:, 10.1038/s41586-020-2389-3. PMID:32494008 doi:http://dx.doi.org/10.1038/s41586-020-2389-3

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6wb9"

@@ Line 3: / Line 3: @@
 <StructureSection load='6wb9' size='340' side='right'caption='[[6wb9]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6wb9]] is a 7 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=6WB9 FirstGlance]. <br>
+<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'>[http://proteopedia.org/fgij/fg.htm?mol=6wb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wb9 OCA], [http://pdbe.org/6wb9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wb9 RCSB], [http://www.ebi.ac.uk/pdbsum/6wb9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wb9 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=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 ==
-[[http://www.uniprot.org/uniprot/EMC5_YEAST EMC5_YEAST]] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [[http://www.uniprot.org/uniprot/EMC2_YEAST EMC2_YEAST]] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [[http://www.uniprot.org/uniprot/EMC6_YEAST EMC6_YEAST]] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [[http://www.uniprot.org/uniprot/EMC1_YEAST EMC1_YEAST]] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [[http://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>  [[http://www.uniprot.org/uniprot/EMC3_YEAST EMC3_YEAST]] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER). [[http://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>  [[http://www.uniprot.org/uniprot/EMC4_YEAST EMC4_YEAST]] The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER).
+[[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 ==

6wb9

From Proteopedia

Current revision

Structure of the S. cerevisiae ER membrane complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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