Crystallization and preliminary crystallographic analysis of dUTPase from the phi 11 helper phage of Staphylococcus aureus

: Leveles I, Rona G, Zagyva I, Bendes A, Harmat V, Vertessy BG

Publisher: INT UNION CRYSTALLOGRAPHY

: 2011

: Acta Crystallographica Section F: Structural Biology Communications

: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS

: ACTA CRYSTALLOGR F

: 67

: 1411

: 1413

: 3

DOI: https://doi.org/10.1107/S1744309111034580

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 phi 11 helper phage has been suggested [Tormo-Mas 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 phi 11 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 angstrom resolution from one type of crystal. The crystal of phi 11 dUTPase belonged to the cubic space group I23, with unit-cell parameters a = 98.16 angstrom, alpha = beta = gamma = 90.00 degrees.