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-Structure paper
タイトル | Two conformations of the Tom20 preprotein receptor in the TOM holo complex. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 120, Issue 34, Page e2301447120, Year 2023 |
掲載日 | 2023年8月22日 |
![]() | Pamela Ornelas / Thomas Bausewein / Janosch Martin / Nina Morgner / Stephan Nussberger / Werner Kühlbrandt / ![]() |
PubMed 要旨 | The TOM complex is the main entry point for precursor proteins (preproteins) into mitochondria. Preproteins containing targeting sequences are recognized by the TOM complex and imported into ...The TOM complex is the main entry point for precursor proteins (preproteins) into mitochondria. Preproteins containing targeting sequences are recognized by the TOM complex and imported into mitochondria. We have determined the structure of the TOM core complex from 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. 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 preproteins 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. |
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手法 | EM (単粒子) |
解像度 | 3.32 - 6.7 Å |
構造データ | EMDB-15849, PDB-8b4i: ![]() EMDB-15850: Cryo-EM structure of the Neurospora crassa TOM core complex with Tom20 over one pore ![]() EMDB-15856: Cryo-EM structure of the Neurospora crassa TOM core complex with Tom20 over both pores |
化合物 | ![]() ChemComp-DU0: ![]() ChemComp-PLC: |
由来 |
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![]() | MEMBRANE PROTEIN / Complex / outer membrane / mitochondria / TOM / translocase / neurospora crassa |