ArticleMolecules and cells2011
Structural insights into the conformational diversity of ClpP from Bacillus subtilis.
Article in Molecules and cells, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 58 citations in OpenAlex.
- Mechanism of allosteric activation in human mitochondrial ClpP protease.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural Insights into Bortezomib-Induced Activation of the Caseinolytic Chaperone-Protease System in Mycobacterium tuberculosis.Nature communications · 2025Article
- Dynamic Oligomerization Processes ofACS omega · 2025Article
- Article
- Molecular insights into the dynamic modulation of bacterial ClpP function and oligomerization by peptidomimetic boronate compounds.Scientific reports · 2024Article
- Antibiotic Acyldepsipeptides Stimulate themBio · 2022Article
- The Nϵ-Rule for Serine, but Not Cysteine Catalytic Triads.Angewandte Chemie (International ed. in English) · 2022Article
- Acyldepsipeptide Analogues: A Future Generation Antibiotics for Tuberculosis Treatment.Pharmaceutics · 2022Review
- Structural insights into ClpP protease side exit pore-opening by a pH drop coupled with substrate hydrolysis.The EMBO journal · 2022Article
- Generation of Lasso Peptide-Based ClpP Binders.International journal of molecular sciences · 2021Article
- Structural basis for the N-degron specificity of ClpS1 from Arabidopsis thaliana.Protein science : a publication of the Protein Society · 2021Article
- Reprogramming of the Caseinolytic Protease by ADEP Antibiotics: Molecular Mechanism, Cellular Consequences, Therapeutic Potential.Frontiers in molecular biosciences · 2021Review
- An allosteric switch regulatesProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Use of the LC3B-fusion technique for biochemical and structural studies of proteins involved in the N-degron pathway.The Journal of biological chemistry · 2020Article
- Acyldepsipeptide Probes Facilitate Specific Detection of Caseinolytic Protease P Independent of Its Oligomeric and Activity State.Chembiochem : a European journal of chemical biology · 2020Article
- Article
- Reversible inhibition of the ClpP protease via an N-terminal conformational switch.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Metabolic Perturbations in a Bacillus subtilis clpP Mutant during Glucose Starvation.Metabolites · 2017Article
- Article
- Structure and Functional Properties of the Active Form of the Proteolytic Complex, ClpP1P2, from Mycobacterium tuberculosis.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ClpP is a cylindrical protease that is tightly regulated by Clp-ATPases. The activation mechanism of ClpP using acyldepsipeptide antibiotics as mimics of natural activators showed enlargement of the axial entrance pore for easier processing of incoming substrates. However, the elimination of degradation products from inside the ClpP chamber remains unclear since there is no exit pore for releasing these products in all determined ClpP structures. Here we report a new crystal structure of ClpP from Bacillus subtilis, which shows a significantly compressed shape along the axial direction. A portion of the handle regions comprising the heptameric ring-ring contacts shows structural transition from an ordered to a disordered state, which triggers the large conformational change from an extended to an overall compressed structure. Along with this structural change, 14 side pores are generated for product release and the catalytic triad adopts an inactive orientation. We have also determined B. subtilis ClpP inhibited by diisopropylfluoro-phosphate and analyzed the active site in detail. Structural information pertaining to several different conformational steps such as those related to extended, ADEP-activated, DFP-inhibited and compressed forms of ClpP from B. subtilis is available. Structural comparisons suggest that functionally important regions in the ClpP-family such as N-terminal segments for the axial pore, catalytic triads, and handle domains for the product releasing pore exhibit intrinsically dynamic and unique structural features. This study provides valuable insights for understanding the enigmatic cylindrical degradation machinery of ClpP as well as other related proteases such as HslV and the 20S proteasome.
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