ArticleNature communications2024
Structural and functional characterization of cyclic pyrimidine-regulated anti-phage system.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Discovery of Small-Molecule Inhibitors of the Pycsar Antiphage Defense.ACS chemical biology · 2026Article
- Manipulation of the nucleotide pool in human, bacterial and plant immunity.Nature reviews. Immunology · 2026Review
- Molecular characterisation of the Bacillus subtilis SpbK antiphage defence system.Nature communications · 2025Article
- Molecular mechanisms of CBASS phospholipase effector CapV mediated membrane disruption.Nature communications · 2025Article
- Structure-guided insights into TIR-mediated bacterial and eukaryotic immunity.Structure (London, England : 1993) · 2025Review
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Authors and funding
5 authors.
Funding
Abstract
3',5'-cyclic uridine monophosphate (cUMP) and 3',5'-cyclic cytidine monophosphate (cCMP) have been established as bacterial second messengers in the phage defense system, named pyrimidine cyclase system for anti-phage resistance (Pycsar). This system consists of a pyrimidine cyclase and a cyclic pyrimidine receptor protein. However, the molecular mechanism underlying cyclic pyrimidine synthesis and recognition remains unclear. Herein, we determine the crystal structures of a uridylate cyclase and a cytidylate cyclase, revealing the conserved residues for cUMP and cCMP production, respectively. In addition, a distinct zinc-finger motif of the uridylate cyclase is identified to confer substantial resistance against phage infections. Furthermore, structural characterization of cUMP receptor protein PycTIR provides clear picture of specific cUMP recognition and identifies a conserved N-terminal extension that mediates PycTIR oligomerization and activation. Overall, our results contribute to the understanding of cyclic pyrimidine-mediated bacterial defense.
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