9I6B

CryoEM structure of the Chaetomium thermophilum TOM core complex at 2.7 angstrom resolution (pALDH treated)

Summary for 9I6B

• Entry DOI: 10.2210/pdb9i6b/pdb
• EMDB information: 52652
• Descriptor: Mitochondrial import receptor subunit tom22, Mitochondrial import receptor subunit tom5, Mitochondrial import receptor subunit tom6, ... (8 entities in total)
• Functional Keywords: mitochondria, membrane protein
• Biological source: Thermochaetoides thermophila DSM 1495; More
• Total number of polymer chains: 10
• Total formula weight: 171761.32

Authors

Agip, A.N.A.,Ornelas, P.,Yang, T.J.,Ermanno, U.,Haeder, S.,McDowell, M.A.,Kuehlbrandt, W. (deposition date: 2025-01-29, release date: 2025-07-09, Last modification date: 2025-07-30)

Primary citation

Agip, A.A.,Ornelas, P.,Yang, T.J.,Uboldi, E.,Hader, S.,McDowell, M.A.,Kuhlbrandt, W.
Structures of Chaetomium thermophilum TOM complexes with bound preproteins.
Proc.Natl.Acad.Sci.USA, 122:e2507279122-e2507279122, 2025

PubMed Abstract: Mitochondria import most of their proteins from the cytoplasm through the TOM complex. Preproteins containing targeting signals are recognized by the TOM receptor subunits and translocated by Tom40 across the outer mitochondrial membrane. We present four structures of the preprotein-bound and preprotein-free TOM core and holo complexes from the thermophilic fungus , obtained by single-particle electron cryomicroscopy. Our structures reveal the symmetric arrangement of two copies of the Tom20 receptor subunit in the TOM holo complex. Several different conformations of Tom20 within the TOM holo complex highlight the dynamic nature of the receptor. The structure of preprotein-bound Tom20 provides insight into the early stages of protein translocation.

PubMed: 40674418
DOI: 10.1073/pnas.2507279122

Experimental method

ELECTRON MICROSCOPY (2.7 Å)