Cryo-EM Structure of the Native GroEL-GroES Complex from Thermus thermophilus Encapsulating Substrate Inside the Cavity
Cryo-EM Structure of the Native GroEL-GroES Complex from Thermus thermophilus Encapsulating Substrate Inside the Cavity
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DOI：
10.1016/j.str.2008.12.012
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发表时间：
2009-02-13
期刊：
影响因子：
5.7
通讯作者：
Mitsuoka, Kaoru
中科院分区：
文献类型：
--
作者：
Kanno, Ryo;Koike-Takeshita, Ayumi;Mitsuoka, Kaoru
伴侣蛋白 GroEL 与各种蛋白质相互作用，导致它们在 GroES 和 ATP 的帮助下采用正确的构象。实际机制仍在争论中。在这项研究中，通过使用冷冻电子显微镜，我们确定了封装其底物蛋白的嗜热栖热菌 GroEL-GroES 复合物的溶液结构。我们观察了 GroEL-GroES 腔中心底物蛋白的平均密度。腔内平均底物密度的位置表明大多数底物蛋白与腔内壁之间存在排斥相互作用，这适合底物释放。此外，我们观察到 cis-GroEL 环的变形，特别是在靠近基底的位置，这表明封装的蛋白质和 GroEL 环之间的相互作用导致空腔形状的调整以适应基底。
The chaperonin GroEL interacts with various proteins, leading them to adopt their correct conformations with the aid of GroES and ATP. The actual mechanism is still being debated. In this study, by use of cryo-electron microscopy, we determined the solution structure of the Thermus thermophilus GroEL-GroES complex encapsulating its substrate proteins. We observed the averaged density of substrate proteins in the center of the GroEL-GroES cavity. The position of the averaged substrate density in the cavity suggested a repulsive interaction between a majority of the substrate proteins and the interior wall of the cavity, which is suitable for substrate release. In addition, we observed a distortion of the cis-GroEL ring, especially at the position near the substrate, which indicated that the interaction between the encapsulated proteins and the GroEL ring results in an adjustment in the cavity's shape to accommodate the substrate.