{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["19"],"submitter":["Araiso Y"],"pubmed_abstract":["Most mitochondrial proteins are synthesized as precursor proteins (preproteins) in the cytosol and imported into mitochondria. The translocator of the outer membrane (TOM) complex functions as a main entry gate for the import of mitochondrial proteins. The TOM complex is a multi-subunit membrane protein complex composed of a β-barrel channel Tom40 and six single-pass membrane proteins. Recent cryo-EM studies have revealed high-resolution structures of the yeast and human TOM complexes, which enabled us to discuss the mechanism of protein import at an amino-acid residue level. The cryo-EM structures show that two Tom40 β-barrels are surrounded by two sets of small Tom subunits to form a dimeric structure. The intermembrane space (IMS) domains of Tom40, Tom22, and Tom7 form a binding site fo"],"journal":["Biophysics and physicobiology"],"pagination":["e190022"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9260164"],"repository":["biostudies-literature"],"pubmed_title":["Structural overview of the translocase of the mitochondrial outer membrane complex."],"pmcid":["PMC9260164"],"pubmed_authors":["Endo T","Araiso Y"],"additional_accession":[]},"is_claimable":false,"name":"Structural overview of the translocase of the mitochondrial outer membrane complex.","description":"Most mitochondrial proteins are synthesized as precursor proteins (preproteins) in the cytosol and imported into mitochondria. The translocator of the outer membrane (TOM) complex functions as a main entry gate for the import of mitochondrial proteins. The TOM complex is a multi-subunit membrane protein complex composed of a β-barrel channel Tom40 and six single-pass membrane proteins. Recent cryo-EM studies have revealed high-resolution structures of the yeast and human TOM complexes, which enabled us to discuss the mechanism of protein import at an amino-acid residue level. The cryo-EM structures show that two Tom40 β-barrels are surrounded by two sets of small Tom subunits to form a dimeric structure. The intermembrane space (IMS) domains of Tom40, Tom22, and Tom7 form a binding site fo","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2025-04-29T10:40:01.655Z","creation":"2025-04-06T19:36:30.947Z"},"accession":"S-EPMC9260164","cross_references":{"pubmed":["35859989"],"doi":["10.2142/biophysico.bppb-v19.0022"]}}