Projects per year
Abstract
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-Å resolution. The structure reveals the high-resolution architecture of the translocator consisting of two Tom40 β-barrel channels and α-helical transmembrane subunits, providing insight into critical features that are conserved in all eukaryotes1–3. Each Tom40 β-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.
Original language | English |
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Pages (from-to) | 395-401 |
Number of pages | 7 |
Journal | Nature |
Volume | 575 |
Issue number | 7782 |
DOIs | |
Publication status | Published - 14 Nov 2019 |
Projects
- 1 Finished
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The molecular blue-print for a mitochondrial nanomachine
Australian Research Council (ARC), Monash University
1/01/16 → 31/12/20
Project: Research