Interaction of complexes I, III, and IV within the bovine respirasome by single particle cryoelectron tomography
Interaction of complexes I, III, and IV within the bovine respirasome by single particle cryoelectron tomography
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DOI：
10.1073/pnas.1107819108
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发表时间：
2011-09-13
影响因子：
11.1
通讯作者：
Boekema, Egbert J.
中科院分区：
文献类型：
--
作者：
Dudkina, Natalya V.;Kudryashev, Mikhail;Boekema, Egbert J.
呼吸酶体是线粒体中呼吸链的多亚基超复合物。在这里，我们报告的3D重建的牛的心脏cardiomasome，由二聚体的复合物III和单拷贝的复合物I和IV，在约2.2 nm的分辨率，确定由冷冻电子断层扫描和子体积平均。拟合的X-射线结构的单一复合物I，III 2，和IV与高保真度允许解释的模型在二级结构的水平，并显示了如何个别复合物内的相互作用的蛋白酶体。令人惊讶的是，复合物III 2和IV的细胞色素c结合位点之间的距离为约10 nm。建模表明三个复合物之间的松散的相互作用，并提供证据表明，脂质粘合它们在接口。
The respirasome is a multisubunit supercomplex of the respiratory chain in mitochondria. Here we report the 3D reconstruction of the bovine heart respirasome, composed of dimeric complex III and single copies of complex I and IV, at about 2.2-nm resolution, determined by cryoelectron tomography and subvolume averaging. Fitting of X-ray structures of single complexes I, III2, and IV with high fidelity allows interpretation of the model at the level of secondary structures and shows how the individual complexes interact within the respirasome. Surprisingly, the distance between cytochrome c binding sites of complexes III2 and IV is about 10 nm. Modeling indicates a loose interaction between the three complexes and provides evidence that lipids are gluing them at the interfaces.