7P6U
Lon protease from Thermus Thermophilus
Summary for 7P6U
| Entry DOI | 10.2210/pdb7p6u/pdb |
| EMDB information | 13232 |
| Descriptor | Lon protease, (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK), PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total) |
| Functional Keywords | bacterial cell division, aaa+, unfolding, protease, cell cycle |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 7 |
| Total formula weight | 539802.40 |
| Authors | Coscia, F.,Lowe, J. (deposition date: 2021-07-18, release date: 2021-10-27, Last modification date: 2025-10-01) |
| Primary citation | Coscia, F.,Lowe, J. Cryo-EM structure of the full-length Lon protease from Thermus thermophilus. Febs Lett., 595:2691-2700, 2021 Cited by 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-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. PubMed: 34591981DOI: 10.1002/1873-3468.14199 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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