Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex.
? barrel outer membrane proteins (?-OMPs) play vital roles in mitochondria, chloroplasts, and Gram-negative bacteria. Evolutionarily conserved complexes such as the mitochondrial sorting and assembly machinery (SAM) mediate the assembly of ?-OMPs. We investigated the SAM-mediated assembly of the translocase of the outer membrane (TOM) core complex. Cryo–electron microscopy structures ... of SAM–fully folded Tom40 and the SAM-Tom40/Tom5/Tom6 complexes at ~3-angstrom resolution reveal that Sam37 stabilizes the mature Tom40 mainly through electrostatic interactions, thus facilitating subsequent TOM assembly. These results support the ? barrel switching model and provide structural insights into the assembly and release of ? barrel complexes.
Mesh Terms:
Carrier Proteins, Cell Line, Cryoelectron Microscopy, Humans, Membrane Proteins, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Mitochondrial Precursor Protein Import Complex Proteins, Models, Molecular, Multiprotein Complexes, Protein Conformation, Protein Folding, Protein Structure, Secondary, Protein Subunits, Protein Transport, Saccharomyces cerevisiae Proteins, Static Electricity
Carrier Proteins, Cell Line, Cryoelectron Microscopy, Humans, Membrane Proteins, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Mitochondrial Precursor Protein Import Complex Proteins, Models, Molecular, Multiprotein Complexes, Protein Conformation, Protein Folding, Protein Structure, Secondary, Protein Subunits, Protein Transport, Saccharomyces cerevisiae Proteins, Static Electricity
Science
Date: Sep. 17, 2021
PubMed ID: 34446444
View in: Pubmed Google Scholar
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