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TitleThe architecture of EMC reveals a path for membrane protein insertion.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateMay 27, 2020
AuthorsJohn P O'Donnell / Ben P Phillips / Yuichi Yagita / Szymon Juszkiewicz / Armin Wagner / Duccio Malinverni / Robert J Keenan / Elizabeth A Miller / Ramanujan S Hegde /
PubMed AbstractApproximately 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 ...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.
External linksElife / PubMed:32459176 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.2 - 6.4 Å
Structure data

11058

6z3w

EMDB-11058: Human ER Membrane protein Complex (EMC)
PDB-6z3w: Human ER membrane protein complex
Method: EM (single particle) / Resolution: 6.4 Å

PDB-6y4l:
Crystal structure of human ER membrane protein complex subunits EMC2 and EMC9
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PE4:
2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL / precipitant*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsPROTEIN TRANSPORT / Complex / insertase / MEMBRANE PROTEIN

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