6UCU

Cryo-EM structure of the mitochondrial TOM complex from yeast (dimer)

6UCU の概要

• エントリーDOI: 10.2210/pdb6ucu/pdb
• EMDBエントリー: 20728 20729
• 分子名称: Mitochondrial import receptor subunit TOM40, Mitochondrial import receptor subunit TOM22, Mitochondrial import receptor subunit TOM5, ... (6 entities in total)
• 機能のキーワード: membrane protein, mitochondrial protein import, mitochondrial outer membrane, protein translocation, translocase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 191695.65

構造登録者

Park, E.,Tucker, K. (登録日: 2019-09-17, 公開日: 2019-11-06, 最終更新日: 2024-03-20)

主引用文献

Tucker, K.,Park, E.
Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution.
Nat.Struct.Mol.Biol., 26:1158-1166, 2019

PubMed Abstract: 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 important acidic patches. The tetrameric complex is essentially a dimer of dimeric TOM, which may be capable of forming higher-order oligomers. Our study reveals the detailed molecular organization of the TOM complex and provides new insights about the mechanism of protein translocation into mitochondria.

PubMed: 31740857
DOI: 10.1038/s41594-019-0339-2

実験手法

ELECTRON MICROSCOPY (3.06 Å)