Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution.,Nature Structural & Molecular Biology

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Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution.
Nature Structural & Molecular Biology ( IF 12.5 ) Pub Date : 2019-11-18 , DOI: 10.1038/s41594-019-0339-2
Kyle Tucker ₁ , Eunyong Park _{1,

2}

Affiliation

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.

中文翻译：

近原子分辨率下线粒体蛋白输入通道 TOM 复合物的冷冻电镜结构。

几乎所有的线粒体蛋白都由核基因组编码，并在胞质核糖体上合成后输入线粒体。这些前体蛋白通过 TOM 复合物（线粒体外膜中的一种蛋白质传导通道）转运到线粒体中。我们已经确定了来自酿酒酵母的二聚体和四聚体形式的核心 TOM 复合物的高分辨率冷冻电镜结构。二聚体 TOM 由 5 种蛋白质中的每一种以双重对称排列的两个拷贝组成：成孔 β-桶蛋白 Tom40 和四种辅助 α-螺旋跨膜蛋白。每个 Tom40 的孔都有一个整体带负电荷的内表面，这归因于多个具有重要功能的酸性斑块。四聚体复合物本质上是二聚体 TOM 的二聚体，它可能能够形成更高阶的寡聚体。

更新日期：2019-11-18

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