Structural basis of protein transport across the outer membrane of human mitochondria (P23)

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The vast majority of mitochondrial proteins are imported to the organelle through the TOM complex, which mediates peptide translocation through the outer membrane. Although recent high-resolution structures of the holo core TOM complex have shed light on the architecture of this multi-subunit pore-forming channel, the molecular mechanisms of cargo recognition, peptide translocation and handover to downstream transport and processing machineries remain unknown. In this project, we will determine structures of actively transporting human TOM complexes bound to different cargo peptides using single-particle cryo-electron microscopy. This will provide molecular insights into the path of the client peptide through the TOM channel and the mechanisms of translocation through the outer mitochondrial membrane.