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Cryo-EM reveals the Trypanosoma brucei ATOM complex structure at 2.8 Å resolution, resolving all known components plus an additional subunit.
- Why it matters: Mitochondrial preprotein import is central to eukaryotic cell function, but how the divergent ATOM machinery evolved from canonical TOM complexes remains unclear.
- What they did: The authors determined the T. brucei ATOM complex cryoelectron microscopy structure at 2.8 Å, mapping the full component set and a newly identified subunit.
- The result: ATOM preserves a conserved dimeric channel and a protein-conducting pathway closely resembling opisthokont TOM, while receptor and intermembrane-space regions show distinct, diversified architectures.
The findingWhy it mattersWhat they didThe result
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