Cryo-EM Structure of the TOM Core Complex from Neurospora crassa.
Cell
; 170(4): 693-700.e7, 2017 Aug 10.
Article
in En
| MEDLINE
| ID: mdl-28802041
ABSTRACT
The TOM complex is the main entry gate for protein precursors from the cytosol into mitochondria. We have determined the structure of the TOM core complex by cryoelectron microscopy (cryo-EM). The complex is a 148 kDa symmetrical dimer of ten membrane protein subunits that create a shallow funnel on the cytoplasmic membrane surface. In the core of the dimer, the ß-barrels of the Tom40 pore form two identical preprotein conduits. Each Tom40 pore is surrounded by the transmembrane segments of the α-helical subunits Tom5, Tom6, and Tom7. Tom22, the central preprotein receptor, connects the two Tom40 pores at the dimer interface. Our structure offers detailed insights into the molecular architecture of the mitochondrial preprotein import machinery.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Fungal Proteins
/
Carrier Proteins
/
Protein Translocation Systems
/
Neurospora crassa
Language:
En
Journal:
Cell
Year:
2017
Type:
Article
Affiliation country:
Germany