Cryo-EM structure of the full-length Lon protease from Thermus thermophilus,FEBS Letters

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Cryo-EM structure of the full-length Lon protease from Thermus thermophilus
FEBS Letters ( IF 3.0 ) Pub Date : 2021-09-30 , DOI: 10.1002/1873-3468.14199
Francesca Coscia ₁ , Jan Löwe ₁

Affiliation

In bacteria, Lon is a large hexameric ATP-dependent protease that targets misfolded and also folded substrates, some of which are involved in cell division and survival of cellular stress. The N-terminal domain of Lon facilitates substrate recognition, but how the domains confer such activity has remained unclear. Here, we report the full-length structure of Lon protease from Thermus thermophilus at 3.9 Å resolution in a substrate-engaged state. The six N-terminal domains are arranged in three pairs, stabilized by coiled-coil segments and forming an additional channel for substrate sensing and entry into the AAA+ ring. Sequence conservation analysis and proteolysis assays confirm that this architecture is required for the degradation of both folded and unfolded substrates in bacteria.

中文翻译：

嗜热栖热菌全长 Lon 蛋白酶的冷冻电镜结构

在细菌中，Lon 是一种大型六聚体 ATP 依赖性蛋白酶，其目标是错误折叠和折叠的底物，其中一些底物参与细胞分裂和细胞应激的生存。 Lon 的 N 端结构域有助于底物识别，但这些结构域如何赋予这种活性仍不清楚。在这里，我们以 3.9 Å 分辨率报道了嗜热栖热菌Lon 蛋白酶在底物接合状态下的全长结构。六个 N 端结构域排列成三对，由卷曲线圈段稳定，并形成用于底物感测和进入 AAA+ 环的附加通道。序列保守分析和蛋白水解测定证实，这种结构是细菌中折叠和未折叠底物降解所必需的。

更新日期：2021-11-08

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