ArticleProceedings of the National Academy of Sciences of the United States of America2007
Structure of the heterotrimeric complex that regulates type III secretion needle formation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 97 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Neutralizing human monoclonal antibodies that target the PcrV component of the type III secretion system ofeLife · 2026Article
- Article
- A Supramolecular Antibiotic Targeting Drug-ResistantACS applied materials & interfaces · 2024Article
- Article
- Assembly mechanism of a Tad secretion system secretin-pilotin complex.Nature communications · 2023Article
- Bcr4 Is a Chaperone for the Inner Rod Protein in theMicrobiology spectrum · 2022Article
- Article
- Direct interaction of a chaperone-bound type III secretion substrate with the export gate.Nature communications · 2022Article
- Delivering the pain: an overview of the type III secretion system with special consideration for aquatic pathogens.Veterinary research · 2021Review
- Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD.Nature communications · 2021Article
- Molecular Targets and Strategies for Inhibition of the Bacterial Type III Secretion System (T3SS); Inhibitors Directly Binding to T3SS Components.Biomolecules · 2021Review
- The PopN Gate-keeper Complex Acts on the ATPase PscN to Regulate the T3SS Secretion Switch from Early to Middle Substrates in Pseudomonas aeruginosa.Journal of molecular biology · 2020Article
- Article
- A Structure-Function-Inhibition Analysis of theJournal of bacteriology · 2020Article
- Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020Review
- The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019Review
- Tanshinones: First-in-Class Inhibitors of the Biogenesis of the Type 3 Secretion System Needle ofACS central science · 2019Article
- Solution Structure of the Carboxy-Terminal Tandem Repeat Domain of Eukaryotic Elongation Factor 2 Kinase and Its Role in Substrate Recognition.Journal of molecular biology · 2019Article
- Chaperone-mediated secretion switching from early to middle substrates in the type III secretion system encoded byThe Journal of biological chemistry · 2019Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type III secretion systems (T3SS), found in several Gram-negative pathogens, are nanomachines involved in the transport of virulence effectors directly into the cytoplasm of target cells. T3SS are essentially composed of basal membrane-embedded ring-like structures and a hollow needle formed by a single polymerized protein. Within the bacterial cytoplasm, the T3SS needle protein requires two distinct chaperones for stabilization before its secretion, without which the entire T3SS is nonfunctional. The 2.0-A x-ray crystal structure of the PscE-PscF(55-85)-PscG heterotrimeric complex from Pseudomonas aeruginosa reveals that the C terminus of the needle protein PscF is engulfed within the hydrophobic groove of the tetratricopeptide-like molecule PscG, indicating that the macromolecular scaffold necessary to stabilize the T3SS needle is totally distinct from chaperoned complexes between pilus- or flagellum-forming molecules. Disruption of specific PscG-PscF interactions leads to impairment of bacterial cytotoxicity toward macrophages, indicating that this essential heterotrimer, which possesses homologs in a wide variety of pathogens, is a unique attractive target for the development of novel antibacterials.
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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.