title: Crystallization and preliminary crystallographic analysis of dUTPase from the φ11 helper phage of Staphylococcus aureus.
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°.
authors.affiliation: Institute of Enzymology, Hungarian Academy of Sciences, Budapest, Hungary. leveles@enzim.hu
authors.forename: Ibolya
authors.initials: I
authors.lastname: Leveles
authors.forename: Gergely
authors.initials: G
authors.lastname: Róna
authors.forename: Imre
authors.initials: I
authors.lastname: Zagyva
authors.forename: Ábris
authors.initials: Á
authors.lastname: Bendes
authors.forename: Veronika
authors.initials: V
authors.lastname: Harmat
authors.forename: Beáta G
authors.initials: BG
authors.lastname: Vértessy
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D011755:Pyrophosphatases / Q000737:chemistry*; D013204:Staphylococcus Phages / Q000201:enzymology*; D013211:Staphylococcus aureus / Q000821:virology*
chemical_list: D011755:Pyrophosphatases; C020020:dUTP pyrophosphatase
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