ArticleThe EMBO journal2010
Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.
Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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Who cites it
47 citing papers in PubMed, 92 citations in OpenAlex.
- Regulation of the Anti-termination RNA Transcription Complex by Lon-Mediated Lambda N Degradation.Advances in experimental medicine and biology · 2026Review
- Mitochondrial proteases and their roles in mitophagy in plants, animals, and yeast.Plant & cell physiology · 2025Review
- Bacteria encode post-mortem protein catabolism that enables altruistic nutrient recycling.Nature communications · 2025Article
- A missense mutation in the barley Xan-h gene encoding the Mg-chelatase subunit I leads to a viable pale green line with reduced daily transpiration rate.Plant cell reports · 2024Article
- Structure, substrate binding and activity of a unique AAA+ protein: the BrxL phage restriction factor.Nucleic acids research · 2023Article
- Roles of LonP1 in Oral-Maxillofacial Developmental Defects and Tumors: A Novel Insight.International journal of molecular sciences · 2022Review
- Unique Structural Fold of LonBA Protease fromInternational journal of molecular sciences · 2022Article
- The mitochondrial unfolded protein response (UPRJournal of hematology & oncology · 2022Review
- Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.Journal of molecular biology · 2022Review
- Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex.Science advances · 2021Article
- Complete three-dimensional structures of the Lon protease translocating a protein substrate.Science advances · 2021Article
- Failure to Guard: Mitochondrial Protein Quality Control in Cancer.International journal of molecular sciences · 2021Review
- Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.Nature communications · 2021Article
- Cryo-EM structure of substrate-freeCurrent research in structural biology · 2019Article
- Akt phosphorylation of mitochondrial Lonp1 protease enables oxidative metabolism and advanced tumor traits.Oncogene · 2019Article
- Crystal structure of the N domain of Lon protease from Mycobacterium avium complex.Protein science : a publication of the Protein Society · 2019Article
- Adaptive homeostasis and the free radical theory of ageing.Free radical biology & medicine · 2018Review
- Multiple domains of bacterial and human Lon proteases define substrate selectivity.Emerging microbes & infections · 2018Article
- A Phosphorylation Switch on Lon Protease Regulates Bacterial Type III Secretion System in Host.mBio · 2018Article
- Mitochondrial LON protease-dependent degradation of cytochrome c oxidase subunits under hypoxia and myocardial ischemia.Biochimica et biophysica acta. Bioenergetics · 2017Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Lon proteases are distributed in all kingdoms of life and are required for survival of cells under stress. Lon is a tandem fusion of an AAA+ molecular chaperone and a protease with a serine-lysine catalytic dyad. We report the 2.0-Å resolution crystal structure of Thermococcus onnurineus NA1 Lon (TonLon). The structure is a three-tiered hexagonal cylinder with a large sequestered chamber accessible through an axial channel. Conserved loops extending from the AAA+ domain combine with an insertion domain containing the membrane anchor to form an apical domain that serves as a gate governing substrate access to an internal unfolding and degradation chamber. Alternating AAA+ domains are in tight- and weak-binding nucleotide states with different domain orientations and intersubunit contacts, reflecting intramolecular dynamics during ATP-driven protein unfolding and translocation. The bowl-shaped proteolytic chamber is contiguous with the chaperone chamber allowing internalized proteins direct access to the proteolytic sites without further gating restrictions.
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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.