ArticleNucleic acids research2017
Viral genome packaging terminase cleaves DNA using the canonical RuvC-like two-metal catalysis mechanism.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Dissecting the dsDNA viral packaging machinery: structural evolution and potential for therapeutics.Journal of virology · 2026Review
- Duck Plague Virus Full-Length UL15 Protein Is a Multifunctional Enzyme Which Not Only Possesses Nuclease Activity but Also Exerts ATPase and DNA-Binding Activity.Veterinary sciences · 2025Article
- Precise and Accurate DNA-3'/5-Ends Polishing withInternational journal of molecular sciences · 2024Article
- Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024Review
- Insights into a viral motor: the structure of the HK97 packaging termination assembly.Nucleic acids research · 2023Article
- Review
- Crystal structure of DNA polymerase I from Thermus phage G20c.Acta crystallographica. Section D, Structural biology · 2022Article
- Molecular Characterization of a DNA Polymerase fromInternational journal of molecular sciences · 2022Article
- Crystal structure and initial characterization of a novel archaeal-like Holliday junction-resolving enzyme from Thermus thermophilus phage Tth15-6.Acta crystallographica. Section D, Structural biology · 2022Article
- Investigation of Pathogenic Mechanism of Covert Mortality Nodavirus Infection inFrontiers in microbiology · 2022Article
- Architecture of the herpesvirus genome-packaging complex and implications for DNA translocation.Protein & cell · 2020Article
- Review
- Cryo-EM structure and in vitro DNA packaging of a thermophilic virus with supersized T=7 capsids.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Non-host class II ribonucleotide reductase in Thermus viruses: sequence adaptation and host interaction.PeerJ · 2019Article
- Porphyrin-Assisted Docking of a Thermophage Portal Protein into Lipid Bilayers: Nanopore Engineering and Characterization.ACS nano · 2017Article
- Structure of the large terminase from a hyperthermophilic virus reveals a unique mechanism for oligomerization and ATP hydrolysis.Nucleic acids research · 2017Article
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10 authors.
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Abstract
Bacteriophages and large dsDNA viruses encode sophisticated machinery to translocate their DNA into a preformed empty capsid. An essential part of this machine, the large terminase protein, processes viral DNA into constituent units utilizing its nuclease activity. Crystal structures of the large terminase nuclease from the thermophilic bacteriophage G20c show that it is most similar to the RuvC family of the RNase H-like endonucleases. Like RuvC proteins, the nuclease requires either Mn2+, Mg2+ or Co2+ ions for activity, but is inactive with Zn2+ and Ca2+. High resolution crystal structures of complexes with different metals reveal that in the absence of DNA, only one catalytic metal ion is accommodated in the active site. Binding of the second metal ion may be facilitated by conformational variability, which enables the two catalytic aspartic acids to be brought closer to each other. Structural comparison indicates that in common with the RuvC family, the location of the two catalytic metals differs from other members of the RNase H family. In contrast to a recently proposed mechanism, the available data do not support binding of the two metals at an ultra-short interatomic distance. Thus we postulate that viral terminases cleave DNA by the canonical RuvC-like mechanism.
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