Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex.
basic_science · Level V
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- Record sourced from PubMed, PMID 34446444.
- Also identified by DOI 10.1126/science.abh0704.
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Abstract
β barrel outer membrane proteins (β-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 β-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 β barrel switching model and provide structural insights into the assembly and release of β barrel complexes.
Medical subject headings
- Carrier Proteins
- Mitochondrial Membrane Transport Proteins
- Mitochondrial Membranes
- Multiprotein Complexes