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Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution

Nat Struct Mol Biol. 2019; 
Tucker K, Park E,
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Proteins, Expression, Isolation and Analysis The samples were analyzed by SDS-PAGE and immunoblotting with anti-Strep (Genscript; A01732) and antiPGK1 (a gift from J. Thorner) antibodies. Standard enhanced chemiluminescence reagents and a Fujifilm LAS-3000 Imager were used for detection Get A Quote

摘要

Nearly all mitochondrial proteins are encoded by the nuclear genome and imported into mitochondria after synthesis on cytosolic ribosomes. These precursor proteins are translocated into mitochondria by the TOM complex, a protein-conducting channel in the mitochondrial outer membrane. We have determined high-resolution cryo-EM structures of the core TOM complex from Saccharomyces cerevisiae in dimeric and tetrameric forms. Dimeric TOM consists of two copies each of five proteins arranged in two-fold symmetry: pore-forming β-barrel protein Tom40 and four auxiliary α-helical transmembrane proteins. The pore of each Tom40 has an overall negatively charged inner surface attributed to multiple functionally importan... More

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