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Structure of the mitochondrial TOM complex revealed by Cryo-EM

August 2017. The TOM complex is the main entry gate for nuclear-encoded mitochondrial proteins into mitochondria. TOM binds and coordinates the transfer of 1000 (yeast) to 1500 (human) different proteins that have a mitochondrial target sequence. Scientists at the Max Planck Institute of Biophysics in Frankfurt 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 β-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. The structure offers detailed insights into the molecular architecture of the mitochondrial preprotein import machinery. More ...

Werner Kühlbrandt, Max Planck Institute of Biophysics, Frankfurt am Main, Germany, werner.kuehlbrandt@biophys.mpg.de


Bausewein T, Mills DJ, Langer JD, Nitschke B, Nussberger S, Kühlbrandt W (2017) Cryo-EM structure of the TOM core complex from Neurospora crassa. Cell 170: 693-700.e7, published online 10 August 2017. http://dx.doi.org/10.1016/j.cell.2017.07.012



Cluster of Excellence Macromolecular Complexes, Frankfurt am Main