Crystallization and preliminary crystallographic analysis of dUTPase from the ?11 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 ?11 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 ?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 Å resolution from one type of crystal. The crystal of ?11 dUTPase belonged to the cubic space group I23, with unit-cell parameters a = 98.16 Å, ? = ? = ? = 90.00°.

SUBMITTER: Leveles I 

PROVIDER: S-EPMC3212463 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature