Cover image: The mitochondrial outer membrane translocase (TOM) recognizes precursor proteins produced in the cytoplasm and binds them for import into the mitochondria. Shown is the atomic model of the N. crassa TOM core complex determined by cryo-EM at 3.3 Å resolution. Two Tom40 β-barrels are tilted ~20° with respect to the membrane normal. Two Tom22 transmembrane helices are positioned between the β-barrels and extend at the intermitochondrial membrane space side of the complex. Two small subunits of Tom5, Tom6 and Tom7 each interact with the two Tom40 barrels.
For reference, see:
- Tracking the activity and position of mitochondrial β-barrel proteins. Wang, S., Nussberger, S. In: Ieva, R. (eds) Transmembrane β-Barrel Proteins. Methods in Molecular Biology, vol 2778. Humana, New York, NY. Cover page: doi.org/10.1007/978-1-0716-3734-0_14 (2024)
- Two conformations of the Tom20 preprotein receptor in the TOM holo complex. Ornelas, P., Bausewein, T., Martin, J., Morgner, N., Nussberger, S. & Kühlbrandt, W. Proceedings of the National Academy of Sciences, USA:120 (34), e23014471, doi: 10.1073/pnas.2301447120 (2023)