ArticleJournal of virology2013
The structure of the NTPase that powers DNA packaging into Sulfolobus turreted icosahedral virus 2.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Structure of NO16, a marine non-tailed vibriophage with an unusual symmetry-mismatched vertex arrangement.PLoS pathogens · 2026Article
- Distribution and Implications of Haloarchaeal Plasmids Disseminated in Self-Encoded Plasmid Vesicles.Microorganisms · 2023Article
- Viruses of theFrontiers in microbiology · 2023Review
- The enigmatic archaeal virosphere.Nature reviews. Microbiology · 2017Review
- Isolation and Characterization of Metallosphaera Turreted Icosahedral Virus, a Founding Member of a New Family of Archaeal Viruses.Journal of virology · 2017Article
- Article
- Structure-Based Mutagenesis of Sulfolobus Turreted Icosahedral Virus B204 Reveals Essential Residues in the Virion-Associated DNA-Packaging ATPase.Journal of virology · 2015Article
- New approach to develop ultra-high inhibitory drug using the power function of the stoichiometry of the targeted nanomachine or biocomplex.Nanomedicine (London, England) · 2015Article
- A structural model of the genome packaging process in a membrane-containing double stranded DNA virus.PLoS biology · 2014Article
- Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea.Nature communications · 2014Article
- Adenosine triphosphatases of thermophilic archaeal double-stranded DNA viruses.Cell & bioscience · 2014Review
- Discovery of a new motion mechanism of biomotors similar to the earth revolving around the sun without rotation.Virology · 2013Review
- Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biochemical reactions powered by ATP hydrolysis are fundamental for the movement of molecules and cellular structures. One such reaction is the encapsidation of the double-stranded DNA (dsDNA) genome of an icosahedrally symmetric virus into a preformed procapsid with the help of a genome-translocating NTPase. Such NTPases have been characterized in detail from both RNA and tailed DNA viruses. We present four crystal structures and the biochemical activity of a thermophilic NTPase, B204, from the nontailed, membrane-containing, hyperthermoacidophilic archaeal dsDNA virus Sulfolobus turreted icosahedral virus 2. These are the first structures of a genome-packaging NTPase from a nontailed, dsDNA virus with an archaeal host. The four structures highlight the catalytic cycle of B204, pinpointing the molecular movement between substrate-bound (open) and empty (closed) active sites. The protein is shown to bind both single-stranded and double-stranded nucleic acids and to have an optimum activity at 80°C and pH 4.5. The overall fold of B204 places it in the FtsK-HerA superfamily of P-loop ATPases, whose cellular and viral members have been suggested to share a DNA-translocating mechanism.
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