New paper in Communications Biology

The binding and hydrolysis of ATP in NLRP3 remains a conundrum: The protein requires ATP for activation, but is not simply activated by excess of nucleotide; how nucleotide exchange is regulated is unclear, as is the correlation of ATP hydrolysis to protein activity. Rebecca and co-workers now analysed the nucleotide binding Walker A and Walker B motifs, sensors 1 and 2, Glu-switch and P-site for their implications in intrinsic hydrolysis and inflammasome activation. This is the first systematic analysis of ATP hydrolysis in STAND ATPases, showing that the correlation of hydrolysis activity to inflammation is multifaceted.