DUF3055 from Staphylococcus aureus adopts unique strategy for structural distinctiveness

Abstract

Staphylococcus aureus remains a public health threat with the WHO classifying the pathogen as a high priority in the development of new antimicrobial agents. Whole genome sequencing has revealed a number of conserved genes that may be essential for cell viability and infection. Characterising the structure and function of these proteins will inevitably aid development of new antimicrobials. Therefore, this study elucidated the structure of hypothetical protein DUF3055 from S. aureus stain Mu50. The protein possesses an as yet undefined function and a unique fold. The size of DUF3055 made it an ideal candidate for NMR characterisation which in conjunction with circular dichroism revealed the protein to be folded. Crystallisation and structural solution found that the overall dimer fold has a negatively charged surface formed by a β-bulge and tightly crossed α-helices, with a complementary size to a DNA single turn. Our structural observations suggest that hypothetical protein DUF3055 from S. aureus has a role in DNA binding and gene regulation.