ArticleJournal of virology2012
The structure of an archaeal viral integrase reveals an evolutionarily conserved catalytic core yet supports a mechanism of DNA cleavage in trans.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Viruses of theFrontiers in microbiology · 2023Review
- Archaeal tyrosine recombinases.FEMS microbiology reviews · 2021Review
- Comparative genetic and genomic analysis of the novel fusellovirus Sulfolobus spindle-shaped virus 10.Virus evolution · 2018Article
- Site-Specific Recombination by SSV2 Integrase: Substrate Requirement and Domain Functions.Journal of virology · 2015Article
- Archaeal extrachromosomal genetic elements.Microbiology and molecular biology reviews : MMBR · 2015Review
- A standardized protocol for the UV induction of Sulfolobus spindle-shaped virus 1.Extremophiles : life under extreme conditions · 2015Article
- Molecular biology of fuselloviruses and their satellites.Extremophiles : life under extreme conditions · 2014Review
- A survey of protein structures from archaeal viruses.Life (Basel, Switzerland) · 2013Review
- The carboxy-terminal αN helix of the archaeal XerA tyrosine recombinase is a molecular switch to control site-specific recombination.PloS one · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The first structure of a catalytic domain from a hyperthermophilic archaeal viral integrase reveals a minimal fold similar to that of bacterial HP1 integrase and defines structural elements conserved across three domains of life. However, structural superposition on bacterial Holliday junction complexes and similarities in the C-terminal tail with that of eukaryotic Flp suggest that the catalytic tyrosine and an additional active-site lysine are delivered to neighboring subunits in trans. An intramolecular disulfide bond contributes significant thermostability in vitro.
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Registered trials
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