Cryo-EM Structure of the TOM Core Complex from Neurospora crassa

Publication date: 10 August 2017
Source:Cell, Volume 170, Issue 4
Author(s): Thomas Bausewein, Deryck J. Mills, Julian D. Langer, Beate Nitschke, Stephan Nussberger, Werner Kühlbrandt
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 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. Our structure offers detailed insights into the molecular architecture of the mitochondrial preprotein import machinery.

Graphical abstract

Teaser

Molecular structure of the TOM preprotein import complex exposes how the two pore assembly translocates proteins into the mitochondria.


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