The translocase of the outer mitochondrial membrane (TOM) is the main entry gate for proteins(1-4). Here we use cryo-electron microscopy to report the structure of the yeast TOM core complex(5-9) at 3.8-angstrom resolution. The structure reveals the high-resolution architecture of the translocator consisting of two Tom40 beta-barrel channels and a-helical transmembrane subunits, providing insight into critical features that are conserved in all eukaryotes(1-3). Each Tom40 beta-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.