ArticleNucleic acids research2019
Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 73 citations in OpenAlex.
- Structural basis of assembly-dependent activation of the MAD3-MAD4 nuclease in the Pseudomonas aeruginosa MADS defense system.Nucleic acids research · 2026Article
- RecBCD Prevents Bacterial Autoimmunity by Clearing Self-DNA Ends Produced During Replication Termination.bioRxiv : the preprint server for biology · 2026Article
- Biochemical Characterization of LsGajA: A Key Nuclease for Gabija Defense in Lactic Acid Bacteria.Microorganisms · 2026Article
- Structural basis of Retron-Eco8-mediated antiphage defense.Nucleic acids research · 2026Article
- Cran1, member of a new class of OLD family ATPases, functions in cell cycle progression in an archaeon.EMBO reports · 2026Article
- The uncharacterizedmicroPublication biology · 2026Article
- Structural basis for Lamassu-based antiviral immunity and its evolution from DNA repair machinery.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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- Specificity and mechanism of tRNA cleavage by the AriB Toprim nuclease of the PARIS bacterial immune system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Structural basis of the RNA-mediated Retron-Eco2 oligomerization.Cell discovery · 2025Article
- A DNA nicking Class 1 OLD family nuclease mediates phage defense in Vibrio cholerae and is countered by a phage-encoded inhibitor.Nucleic acids research · 2025Article
- Unveiling the multifaceted domain polymorphism of the Menshen antiphage system.Nucleic acids research · 2025Article
- AmBio · 2024Article
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- Molecular basis of Gabija anti-phage supramolecular assemblies.Nature structural & molecular biology · 2024Article
- DdmABC-dependent death triggered by viral palindromic DNA sequences.Cell reports · 2024Article
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- Knowing Our Enemy in the Antimicrobial Resistance Era: Dissecting the Molecular Basis of Bacterial Defense Systems.International journal of molecular sciences · 2024Review
- Structural and biochemical insights into the mechanism of the Gabija bacterial immunity system.Nature communications · 2024Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Overcoming lysogenization defect (OLD) proteins constitute a family of uncharacterized nucleases present in bacteria, archaea, and some viruses. These enzymes contain an N-terminal ATPase domain and a C-terminal Toprim domain common amongst replication, recombination, and repair proteins. The in vivo activities of OLD proteins remain poorly understood and no definitive structural information exists. Here we identify and define two classes of OLD proteins based on differences in gene neighborhood and amino acid sequence conservation and present the crystal structures of the catalytic C-terminal regions from the Burkholderia pseudomallei and Xanthamonas campestris p.v. campestris Class 2 OLD proteins at 2.24 Å and 1.86 Å resolution respectively. The structures reveal a two-domain architecture containing a Toprim domain with altered architecture and a unique helical domain. Conserved side chains contributed by both domains coordinate two bound magnesium ions in the active site of B. pseudomallei OLD in a geometry that supports a two-metal catalysis mechanism for cleavage. The spatial organization of these domains additionally suggests a novel mode of DNA binding that is distinct from other Toprim containing proteins. Together, these findings define the fundamental structural properties of the OLD family catalytic core and the underlying mechanism controlling nuclease activity.
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