ArticleNucleic acids research2020
NMR structure of a vestigial nuclease provides insight into the evolution of functional transitions in viral dsDNA packaging motors.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- 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
- Regulation of the ordinal DNA translocation cycle in bacteriophage Φ29 through trans-subunit interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Origin, Evolution and Diversity of φ29-like Phages-Review and Bioinformatic Analysis.International journal of molecular sciences · 2024Review
- Biophysical and structural characterization of a multifunctional viral genome packaging motor.Nucleic acids research · 2024Article
- Insights into a viral motor: the structure of the HK97 packaging termination assembly.Nucleic acids research · 2023Article
- Revolving hexameric ATPases as asymmetric motors to translocate double-stranded DNA genome along one strand.iScience · 2023Review
- Atomistic basis of force generation, translocation, and coordination in a viral genome packaging motor.Nucleic acids research · 2021Article
- The PLB measurement for the connector in Phi29 bacteriophage reveals the function of its channel loop.Biophysical journal · 2021Article
- A viral genome packaging motor transitions between cyclic and helical symmetry to translocate dsDNA.Science advances · 2021Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Double-stranded DNA viruses use ATP-powered molecular motors to package their genomic DNA. To ensure efficient genome encapsidation, these motors regulate functional transitions between initiation, translocation, and termination modes. Here, we report structural and biophysical analyses of the C-terminal domain of the bacteriophage phi29 ATPase (CTD) that suggest a structural basis for these functional transitions. Sedimentation experiments show that the inter-domain linker in the full-length protein promotes oligomerization and thus may play a role in assembly of the functional motor. The NMR solution structure of the CTD indicates it is a vestigial nuclease domain that likely evolved from conserved nuclease domains in phage terminases. Despite the loss of nuclease activity, fluorescence binding assays confirm the CTD retains its DNA binding capabilities and fitting the CTD into cryoEM density of the phi29 motor shows that the CTD directly binds DNA. However, the interacting residues differ from those identified by NMR titration in solution, suggesting that packaging motors undergo conformational changes to transition between initiation, translocation, and termination. Taken together, these results provide insight into the evolution of functional transitions in viral dsDNA packaging motors.
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