ArticleNature structural & molecular biology2024
PtuA and PtuB assemble into an inflammasome-like oligomer for anti-phage defense.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Structural basis of assembly-dependent activation of the MAD3-MAD4 nuclease in the Pseudomonas aeruginosa MADS defense system.Nucleic acids research · 2026Article
- Phage hijacks host phosphorothioate DNA modification machinery to circumvent bacterial Ssp defences.Nature microbiology · 2026Article
- Review
- Octameric dGTPase assemblies mediate broad anti-phage defense.Nature communications · 2026Article
- Structural and enzymatic insights into QatD, a dual-function TatD-like nuclease in the QatABCD anti-phage defense system.Nucleic acids research · 2026Article
- Structural investigation of QatB and QatC proteins in QatABCD anti-phage defense.Nature communications · 2026Article
- Structural insights into the assembly and function of Retron Ec78 PtuAB.Communications biology · 2026Article
- Phage homing endonuclease amplifies anti-defense genes to evade bacterial immunity.Nature communications · 2026Article
- Tmn blocks phage spread via plasmolysis and triggers synergistic defence responses.bioRxiv : the preprint server for biology · 2026Article
- Article
- Review
- Isolation, characterization and genomic analysis of a novel lytic bacteriophage EcoPhCCP1, capable of infecting multiple strains of multidrug-resistantThe Journal of general virology · 2026Article
- [Research on Bacteriophage Resistance: Coevolutionary Arms Race Between Bacteria and Phages Drives Novel Antibacterial Therapies].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2026Review
- Bacterial defense systems: Mechanisms, homology to eukaryotic immune systems, and applications.Zoological research · 2026Review
- Revisiting lactococcal abortive infection-like antiphage systems: diversity, structures, and mechanisms.FEMS microbiology reviews · 2026Review
- Structural basis for retron co-option of anti-phage ATPase-nuclease.Nature structural & molecular biology · 2026Article
- Characterization and diversity of defense systems inFrontiers in immunology · 2026Article
- Architecture and mechanism of a dual-enzyme retron system in prokaryotic immunity.Nature communications · 2025Article
- Structural mechanism of the Retron-Eco7 anti-phage defense system.Nature communications · 2025Article
- Argonaute-HNH filaments triggered by invader DNA confer bacterial immunity.Nature communications · 2025Article
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15 authors.
Funding
Abstract
Escherichia coli Septu system, an anti-phage defense system, comprises two components: PtuA and PtuB. PtuA contains an ATPase domain, while PtuB is predicted to function as a nuclease. Here we show that PtuA and PtuB form a stable complex with a 6:2 stoichiometry. Cryo-electron microscopy structure of PtuAB reveals a distinctive horseshoe-like configuration. PtuA adopts a hexameric arrangement, organized as an asymmetric trimer of dimers, contrasting the ring-like structure by other ATPases. Notably, the three pairs of PtuA dimers assume distinct conformations and fulfill unique roles in recruiting PtuB. Our functional assays have further illuminated the importance of the oligomeric assembly of PtuAB in anti-phage defense. Moreover, we have uncovered that ATP molecules can directly bind to PtuA and inhibit the activities of PtuAB. Together, the assembly and function of the Septu system shed light on understanding other ATPase-containing systems in bacterial immunity.
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