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The structure of the TOM core complex in the mitochondrial outer membrane

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Bausewein,  Thomas
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Bausewein, T., Naveed, H., Liang, J., & Nussberger, S. (2020). The structure of the TOM core complex in the mitochondrial outer membrane. Biological Chemistry, 401(6-7), 687-697. doi:10.1515/hsz-2020-0104.


Cite as: http://hdl.handle.net/21.11116/0000-0006-ABE2-A
Abstract
In the past three decades, significant advances have been made in providing the biochemical background of TOM (translocase of the outer mitochondrial membrane)-mediated protein translocation into mitochondria. In the light of recent cryoelectron microscopy-derived structures of TOM isolated from Neurospora crassa and Saccharomyces cerevisiae, the interpretation of biochemical and biophysical studies of TOM-mediated protein transport into mitochondria now rests on a solid basis. In this review, we compare the subnanometer structure of N. crassa TOM core complex with that of yeast. Both structures reveal remarkably well-conserved symmetrical dimers of 10 membrane protein subunits. The structural data also validate predictions of weakly stable regions in the transmembrane β-barrel domains of the protein-conducting subunit Tom40, which signal the existence of β-strands located in interfaces of protein-protein interactions.