Practice question

RuvB belongs to AAA+ ATPase superfamily associated with various cellular activities containing Walker A and Walker B motifs required for ATP binding and hydrolysis. It forms hexameric ring structures that encircle double-stranded DNA adjacent to RuvA-bound junction. ATP binding stabilizes oligomer on DNA, while hydrolysis drives rotation and translocation pulling DNA through RuvA scaffold. This motor activity powers ATP-dependent branch migration extending heteroduplex length without requiring strand cleavage. Mutation of Walker motifs eliminates ATPase activity and stalls recombination intermediate processing, demonstrating essential helicase-like function distinct from endonucleolytic resolution.