Structure of the mitochondrial import gate reveals distinct preprotein paths.

The translocase of the outer mitochondrial membrane (TOM) is the main entry gate for proteins1-4. Here we use cryo-electron microscopy to report the structure of the yeast TOM core complex5-9 at 3.8-A resolution. The structure reveals the high-resolution architecture of the translocator consisting of two Tom40 ?-barrel channels and ?-helical ...
transmembrane subunits, providing insight into critical features that are conserved in all eukaryotes1-3. Each Tom40 ?-barrel is surrounded by small TOM subunits, and tethered by two Tom22 subunits and one phospholipid. The N-terminal extension of Tom40 forms a helix inside the channel; mutational analysis reveals its dual role in early and late steps in the biogenesis of intermembrane-space proteins in cooperation with Tom5. Each Tom40 channel possesses two precursor exit sites. Tom22, Tom40 and Tom7 guide presequence-containing preproteins to the exit in the middle of the dimer, whereas Tom5 and the Tom40 N extension guide preproteins lacking a presequence to the exit at the periphery of the dimer.
Mesh Terms:
Cryoelectron Microscopy, Mitochondria, Mitochondrial Membrane Transport Proteins, Models, Molecular, Phospholipids, Protein Multimerization, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Nature
Date: Dec. 01, 2018
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