TOM holo compex cryoEM structure on PNAS cover

August 20, 2023 /

Single-particle average structures of the mitochondrial outer membrane translocase in a detergent micelle

Cover image: The mitochondrial outer membrane translocase (TOM) recognizes and primes precursor proteins produced in the cytoplasm for import into mitochondria. Pictured are single-particle average structures of the  TOM holo complex in a detergent micelle.

For references, see 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) (Journal cover) .

Pamela Ornelas et al. used single-particle electron cryomicroscopy to image the TOM core complex from Neurospora crassa by single-particle electron cryomicroscopy at 3.3 Å resolution, showing its interaction with a bound preprotein at 4 Å resolution, and of the TOM holo complex including the Tom20 receptor at 6 to 7 Å resolution.

Image credit: Pamela Ornelas





Biophysics Group, Institute of Biomaterials and biomolecular Systems, University of Stuttgart

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