Cryo-EM Structure of the TOM Core Complex from Neurospora crassa
Cryo-EM Structure of the TOM Core Complex from Neurospora crassa
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DOI：
10.1016/j.cell.2017.07.012
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发表时间：
2017-08-10
期刊：
影响因子：
64.5
通讯作者：
Kuehlbrandt, Werner
中科院分区：
文献类型：
--
作者：
Bausewein, Thomas;Mills, Deryck J.;Kuehlbrandt, Werner
TOM复合物是蛋白质前体从细胞质进入线粒体的主要入口。我们通过冷冻电镜（cryo - EM）确定了TOM核心复合物的结构。该复合物是由10个膜蛋白亚基组成的148 kDa对称二聚体，在细胞质膜表面形成一个浅漏斗。在二聚体的核心，Tom40孔的β - 桶结构形成两个相同的前体蛋白通道。每个Tom40孔都被α - 螺旋亚基Tom5、Tom6和Tom7的跨膜片段所环绕。中心前体蛋白受体Tom22在二聚体界面连接两个Tom40孔。我们的结构为线粒体前体蛋白输入机制的分子结构提供了详细的见解。
The TOM complex is the main entry gate for protein precursors from the cytosol into mitochondria. We have determined the structure of the TOM core complex by cryoelectron microscopy (cryo-EM). The complex is a 148 kDa symmetrical dimer of ten membrane protein subunits that create a shallow funnel on the cytoplasmic membrane surface. In the core of the dimer, the beta-barrels of the Tom40 pore form two identical preprotein conduits. Each Tom40 pore is surrounded by the transmembrane segments of the alpha-helical subunits Tom5, Tom6, and Tom7. Tom22, the central preprotein receptor, connects the two Tom40 pores at the dimer interface. Our structure offers detailed insights into the molecular architecture of the mitochondrial preprotein import machinery.