Structural highlights
Function
[TOM40_NEUCR] Channel-forming protein essential for import of protein precursors into mitochondria.[1]
Publication Abstract from PubMed
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 beta-barrels of the Tom40 pore form two identical preprotein conduits. Each Tom40 pore is surrounded by the transmembrane segments of the alpha-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.
Cryo-EM Structure of the TOM Core Complex from Neurospora crassa.,Bausewein T, Mills DJ, Langer JD, Nitschke B, Nussberger S, Kuhlbrandt W Cell. 2017 Aug 10;170(4):693-700.e7. doi: 10.1016/j.cell.2017.07.012. PMID:28802041[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ahting U, Thieffry M, Engelhardt H, Hegerl R, Neupert W, Nussberger S. Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria. J Cell Biol. 2001 Jun 11;153(6):1151-60. PMID:11402060
- ↑ Bausewein T, Mills DJ, Langer JD, Nitschke B, Nussberger S, Kuhlbrandt W. Cryo-EM Structure of the TOM Core Complex from Neurospora crassa. Cell. 2017 Aug 10;170(4):693-700.e7. doi: 10.1016/j.cell.2017.07.012. PMID:28802041 doi:http://dx.doi.org/10.1016/j.cell.2017.07.012
