ArticlemBio2019
Structural Basis for the Differential Regulatory Roles of the PDZ Domain in C-Terminal Processing Proteases.
Article in mBio, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- Structures of Helicobacter pylori C-terminal protease CtpA reveal a new mode of self-contained proteolytic processing.Communications biology · 2025Article
- Periplasmic protein quality control at atomic level in live cells.Nature communications · 2025Article
- A periplasmic protein modulates the proteolysis of peptidoglycan hydrolases to maintain cell wall homeostasis inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cleavage of an engulfment peptidoglycan hydrolase by a sporulation signature protease in Clostridioides difficile.Molecular microbiology · 2024Article
- Structural basis for recruitment of peptidoglycan endopeptidase MepS by lipoprotein NlpI.Nature communications · 2024Article
- P. aeruginosa CtpA protease adopts a novel activation mechanism to initiate the proteolytic process.The EMBO journal · 2024Article
- NlpI-Prc Proteolytic Complex Mediates Peptidoglycan Synthesis and Degradation via Regulation of Hydrolases and Synthases inInternational journal of molecular sciences · 2023Article
- In-cell kinetic stability is an essential trait in metallo-β-lactamase evolution.Nature chemical biology · 2023Article
- Article
- Bacterial Carboxyl-Terminal Processing Proteases Play Critical Roles in the Cell Envelope and Beyond.Journal of bacteriology · 2022Review
- Processing of D1 Protein: A Mysterious Process Carried Out in Thylakoid Lumen.International journal of molecular sciences · 2022Review
- Article
- Direct and Indirect Interactions Promote Complexes of the Lipoprotein LbcA, the CtpA Protease and Its Substrates, and Other Cell Wall Proteins in Pseudomonas aeruginosa.Journal of bacteriology · 2021Article
- Inherently and Conditionally Essential Protein Catabolism Genes of Porphyromonas gingivalis.Trends in microbiology · 2021Review
- The C-terminus of substrates is critical but not sufficient for their degradation by theJournal of bacteriology · 2020Article
- Mutation of the Carboxy-Terminal Processing Protease inPathogens (Basel, Switzerland) · 2020Article
- Role of Regulated Proteolysis in the Communication of Bacteria With the Environment.Frontiers in molecular biosciences · 2020Review
- Identification of MltG as a Prc Protease Substrate Whose Dysregulation Contributes to the Conditional Growth Defect of Prc-DeficientFrontiers in microbiology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carboxyl (C)-terminal processing proteases (CTPs) participate in protective and regulatory proteolysis in bacteria. The PDZ domain is central to the activity of CTPs but plays inherently different regulatory roles. For example, the PDZ domain inhibits the activity of the signaling protease CtpB by blocking the active site but is required for the activation of Prc (or Tsp), a tail-specific protease that degrades SsrA-tagged proteins. Here, by structural and functional analyses, we show that in the unliganded resting state of Prc, the PDZ domain is docked inside the bowl-shaped scaffold without contacting the active site, which is kept in a default misaligned conformation. In Prc, a hydrophobic substrate sensor distinct from CtpB engages substrate binding to the PDZ domain and triggers a structural remodeling to align the active-site residues. Therefore, this work reveals the structural basis for understanding the contrasting roles of the PDZ domain in the regulation of CTPs.
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