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-Structure paper
タイトル | Cryo-EM structure of the full-length Lon protease from Thermus thermophilus. |
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ジャーナル・号・ページ | FEBS Lett, Vol. 595, Issue 21, Page 2691-2700, Year 2021 |
掲載日 | 2021年10月18日 |
著者 | Francesca Coscia / Jan Löwe / |
PubMed 要旨 | 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. |
リンク | FEBS Lett / PubMed:34591981 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.9 Å |
構造データ | EMDB-13232, PDB-7p6u: |
化合物 | ChemComp-ANP: |
由来 |
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キーワード | CELL CYCLE (細胞周期) / bacterial cell division / AAA+ / unfolding / protease (プロテアーゼ) |