TY  - INPR
A1  - Ornelas, Pamela
A1  - Bausewein, Thomas
A1  - Martin, Janosch
A1  - Morgner, Nina
A1  - Nußberger, Stephan
A1  - Kühlbrandt, Werner
T1  - Two conformations of the Tom20 preprotein receptor in the TOM holo complex
T2  - bioRxiv
N2  - The TOM complex is the main entry point for precursor proteins into mitochondria. Precursor proteins containing targeting sequences are recognized by the TOM complex and imported into the mitochondria. We have determined the structure of the TOM core complex from Neurospora crassa by single-particle cryoEM at 3.3 Å resolution, showing its interaction with a bound presequence at 4 Å resolution, and of the TOM holo complex including the Tom20 receptor at 6-7 Å resolution. TOM is a transmembrane complex consisting of two β-barrels, three receptor subunits and three short transmembrane subunits. Tom20 has a transmembrane helix and a receptor domain on the cytoplasmic side. We propose that Tom20 acts as a dynamic gatekeeper, guiding precursor proteins into the pores of the TOM complex. We analyze the interactions of Tom20 with other TOM subunits, present insights into the structure of the TOM holo complex, and suggest a translocation mechanism.
Y1  - 2023
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/73163
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-731636
IS  - 2023.01.26.525638
ER  -