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

FEBS Letters

article

Francesca Coscia¹  Jan Löwe¹ 

[1] MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus

关键词: AAA+;    cell cycle;    coiled-coil;    Lon;    protease;    unfolding;   

DOI  :  10.1002/1873-3468.14199

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown