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| Title | Cryo-EM structure of the full-length Lon protease from Thermus thermophilus. |
|---|---|
| Journal, issue, pages | FEBS Lett, Vol. 595, Issue 21, Page 2691-2700, Year 2021 |
| Publish date | Oct 18, 2021 |
 Authors | Francesca Coscia / Jan Löwe /  |
| PubMed Abstract | 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- ...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. |
 External links | FEBS Lett / PubMed:34591981 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.9 Å |
| Structure data | EMDB-13232, PDB-7p6u: |
| Chemicals |  ChemComp-ANP: |
| Source |
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 Keywords | CELL CYCLE / bacterial cell division / AAA+ / unfolding / protease |
thermus thermophilus (bacteria)