ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Crystallization and preliminary crystallographic analysis of dUTPase from the φ11 helper phage of Staphylococcus aureus.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 4 citations in OpenAlex.
- dUTPase modulates mycobacterial homologous recombination and interacts with the AdnAB helicase-nuclease.Nucleic acids research · 2026Article
- Evidence-Based Structural Model of the Staphylococcal Repressor Protein: Separation of Functions into Different Domains.PloS one · 2015Article
- Highly potent dUTPase inhibition by a bacterial repressor protein reveals a novel mechanism for gene expression control.Nucleic acids research · 2014Article
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6 authors at 3 institutions in 1 country.
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Abstract
Staphylococcus aureus superantigen-carrying pathogenicity islands (SaPIs) play a determinant role in spreading virulence genes among bacterial populations that constitute a major health hazard. Repressor (Stl) proteins are responsible for the transcriptional regulation of pathogenicity island genes. Recently, a derepressing interaction between the repressor Stl SaPIbov1 and dUTPase from the φ11 helper phage has been suggested [Tormo-Más et al. (2010), Nature (London), 465, 779-782]. Towards elucidation of the molecular mechanism of this interaction, this study reports the expression, purification and X-ray analysis of φ11 dUTPase, which contains a phage-specific polypeptide segment that is not present in other dUTPases. Crystals were obtained using the hanging-drop vapour-diffusion method at room temperature. Data were collected to 2.98 Å resolution from one type of crystal. The crystal of φ11 dUTPase belonged to the cubic space group I23, with unit-cell parameters a = 98.16 Å, α = β = γ = 90.00°.
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