Structural analysis of the 26S proteasome by cryoelectron tomography
Structural analysis of the 26S proteasome by cryoelectron tomography
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DOI：
10.1016/j.bbrc.2006.11.141
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发表时间：
2007-02-02
影响因子：
3.1
通讯作者：
Baumeister, Wolfgang
中科院分区：
文献类型：
--
作者：
Nickell, Stephan;Mihalache, Oana;Baumeister, Wolfgang
26S蛋白酶体是真核细胞内蛋白质降解的关键酶。它是 2.5 MDa 的多亚基复合物，将蛋白水解作用限制在具有严格控制通道的内部隔室中。这种有趣的分子机器的结构研究因其固有的不稳定性和动力学而受到阻碍。在这里，我们使用了一种非常规方法来获得全复合物的三维结构，不受制备引起的改变的影响，并且不受任何起始模型的影响。我们进行了断层扫描重建，然后对大约约进行了平均。悬浮在薄薄的无定形冰层中的果蝇 26S 蛋白酶体的 150 个个体重建。 (c) 2006 Elsevier Inc. 保留所有权利。
The 26S proteasome is the key enzyme of intracellular protein degradation in eukaryotic cells. It is a multisubunit complex of 2.5 MDa confining the proteolytic action to an inner compartment with tightly controlled access. Structural studies of this intriguing molecular machine have been hampered by its intrinsic instability and its dynamics. Here we have used an unconventional approach to obtain a three-dimensional structure of the holocomplex uncompromised by preparation-induced alterations and unbiased by any starting model. We have performed a tomographic reconstruction, followed by averaging over approx. 150 individual reconstructions, of Drosophila 26S proteasomes suspended in a thin layer of amorphous ice. (c) 2006 Elsevier Inc. All rights reserved.