- PDB-6y4l: Crystal structure of human ER membrane protein complex subunits E... -
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Basic information
Entry
Database: PDB / ID: 6y4l
Title
Crystal structure of human ER membrane protein complex subunits EMC2 and EMC9
Components
(ER membrane protein complex subunit ...) x 2
Keywords
PROTEIN TRANSPORT / Complex / insertase
Function / homology
Function and homology information
extrinsic component of endoplasmic reticulum membrane / EMC complex / protein insertion into ER membrane by stop-transfer membrane-anchor sequence / tail-anchored membrane protein insertion into ER membrane / endoplasmic reticulum membrane / endoplasmic reticulum / cytoplasm Similarity search - Function
ER membrane protein complex subunit 8/9 / Uncharacterised protein family (UPF0172) / ER membrane protein complex subunit 2-like / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / MPN domain / MPN domain profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / ER membrane protein complex subunit 2 / ER membrane protein complex subunit 9 Similarity search - Component
Biological species
Homo sapiens (human)
Method
X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.2 Å
Journal: Elife / Year: 2020 Title: The architecture of EMC reveals a path for membrane protein insertion. Authors: John P O'Donnell / Ben P Phillips / Yuichi Yagita / Szymon Juszkiewicz / Armin Wagner / Duccio Malinverni / Robert J Keenan / Elizabeth A Miller / Ramanujan S Hegde / Abstract: 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 ...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.
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