4. März 2020 /

The structure of the TOM core complex in the mitochondrial outer membrane. Bausewein et al. (2020) Biological Chemistry

In the past three decades, significant advances have been made in providing the biochemical background of TOM-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 sub-nanometer structure of N. crassa TOM core complex with that of yeast. Both structures reveal remarkably well-conserved symmetrical dimers of ten membrane protein subunits. The structural data also validate predictions of weakly stable regions in the transmembrane beta-barrel domains of the protein-conducting subunit Tom40, which signal the existence of beta-strands located in interfaces of protein-protein interactions.

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

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