ArticleNature communications2024
Structural insight into the distinct regulatory mechanism of the HEPN-MNT toxin-antitoxin system in Legionella pneumophila.
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 4 papers.
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Who cites it
4 citing papers in PubMed.
- Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.Structure (London, England : 1993) · 2026Article
- Ribosomal RNA cleavage by the previously unidentified RelS-RelI toxin-antitoxin system controls growth of Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- The Enzymatic Mechanism of OAS: How Metal Ions and Quantum Effects Help Activate Innate Immunity.ACS omega · 2026Article
- Dual regulation of HEPN RNase in fused MNT-HEPN toxin-antitoxin systems via protein OligoAMPylation and oligomerization.Nucleic acids research · 2026Article
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Authors and funding
10 authors.
Funding
Abstract
HEPN-MNT, a type VII TA module, comprises the HEPN toxin and the MNT antitoxin, which acts as a nucleotidyltransferase that transfers the NMP moiety to the corresponding HEPN toxin, thereby interfering with its toxicity. Here, we report crystal structures of the Legionella pneumophila HEPN-MNT module, including HEPN, AMPylated HEPN, MNT, and the HEPN-MNT complex. Our structural analysis and biochemical assays, suggest that HEPN is a metal-dependent RNase and identify its active site residues. We also elucidate the oligomeric state of HEPN in solution. Interestingly, L. pneumophila MNT, which lacks a long C-terminal α4 helix, controls the toxicity of HEPN toxin via a distinct binding mode with HEPN. Finally, we propose a comprehensive regulatory mechanism of the L. pneumophila HEPN-MNT module based on structural and functional studies. These results provide insight into the type VII HEPN-MNT TA system.
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