ArticleJournal of molecular biology2012
The structures of coiled-coil domains from type III secretion system translocators reveal homology to pore-forming toxins.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 66 citations in OpenAlex.
- Protein-centric mechanisms of typhoidalFrontiers in cellular and infection microbiology · 2026Review
- Targeting Type III Secretion System usingIndian journal of microbiology · 2025Review
- Speaking the host language: howMicrobiology (Reading, England) · 2023Review
- Cryo-EM of the injectisome and type III secretion systems.Current opinion in structural biology · 2022Review
- Cryo-EM structure of the needle filament tip complex of theProceedings of the National Academy of Sciences of the United States of America · 2021Article
- TheMicroorganisms · 2021Review
- Review
- Structural Insights ofFrontiers in cellular and infection microbiology · 2021Article
- The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019Review
- On the road to structure-based development of anti-virulence therapeutics targeting the type III secretion system injectisome.MedChemComm · 2019Review
- Article
- Role of SpaO in the assembly of the sorting platform of a Salmonella type III secretion system.PLoS pathogens · 2019Article
- Using disruptive insertional mutagenesis to identify the in situ structure-function landscape of the Shigella translocator protein IpaB.Protein science : a publication of the Protein Society · 2018Article
- Article
- Acylation of the Type 3 Secretion System Translocon Using a Dedicated Acyl Carrier Protein.PLoS genetics · 2017Article
- Characterization of V. cholerae T3SS-dependent cytotoxicity in cultured intestinal epithelial cells.Cellular microbiology · 2016Article
- Article
- Genetic Dissection of the Signaling Cascade that Controls Activation of the Shigella Type III Secretion System from the Needle Tip.Scientific reports · 2016Article
- Characterization of the Binding of Hydroxyindole, Indoleacetic acid, and Morpholinoaniline to the Salmonella Type III Secretion System Proteins SipD and SipB.ChemMedChem · 2016Article
- Characterization of the Shigella and Salmonella Type III Secretion System Tip-Translocon Protein-Protein Interaction by Paramagnetic Relaxation Enhancement.Chembiochem : a European journal of chemical biology · 2016Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Many pathogenic Gram-negative bacteria utilize type III secretion systems (T3SSs) to alter the normal functions of target cells. Shigella flexneri uses its T3SS to invade human intestinal cells to cause bacillary dysentery (shigellosis) that is responsible for over one million deaths per year. The Shigella type III secretion apparatus is composed of a basal body spanning both bacterial membranes and an exposed oligomeric needle. Host altering effectors are secreted through this energized unidirectional conduit to promote bacterial invasion. The active needle tip complex of S. flexneri is composed of a tip protein, IpaD, and two pore-forming translocators, IpaB and IpaC. While the atomic structure of IpaD has been elucidated and studied, structural data on the hydrophobic translocators from the T3SS family remain elusive. We present here the crystal structures of a protease-stable fragment identified within the N-terminal regions of IpaB from S. flexneri and SipB from Salmonella enterica serovar Typhimurium determined at 2.1 Å and 2.8 Å limiting resolution, respectively. These newly identified domains are composed of extended-length (114 Å in IpaB and 71 Å in SipB) coiled-coil motifs that display a high degree of structural homology to one another despite the fact that they share only 21% sequence identity. Further structural comparisons also reveal substantial similarity to the coiled-coil regions of pore-forming proteins from other Gram-negative pathogens, notably, colicin Ia. This suggests that these mechanistically separate and functionally distinct membrane-targeting proteins may have diverged from a common ancestor during the course of pathogen-specific evolutionary events.
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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.