ArticleFEBS letters2021
Cryo-EM structure of the full-length Lon protease from Thermus thermophilus.
Article in FEBS letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Mrx6 binds the Lon protease Pim1 N-terminal domain to confer selective substrate specificity and regulate mtDNA copy number.Nucleic acids research · 2026Article
- Substrate-dependent activation of LONP1 informs on proteolytic regulation and ATPase motor function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cryo-EM Reveals Regulatory Mechanisms Governing Substrate Selection and Activation of Human LONP1.bioRxiv : the preprint server for biology · 2025Article
- Article
- Structural basis for the allosteric activation of Lon by the heat shock protein LarA.Nature communications · 2025Article
- Bacteria encode post-mortem protein catabolism that enables altruistic nutrient recycling.Nature communications · 2025Article
- Structural and mechanistic studies on human LONP1 redefine the hand-over-hand translocation mechanism.bioRxiv : the preprint server for biology · 2024Article
- A 5+1 assemble-to-activate mechanism of the Lon proteolytic machine.Nature communications · 2023Article
- Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate.Nature communications · 2023Article
- Structure, Substrate Specificity and Role of Lon Protease in Bacterial Pathogenesis and Survival.International journal of molecular sciences · 2023Review
- Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.Journal of molecular biology · 2022Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.