Thank you Anthony! I hope you enjoy the reading ;)

We explored the role of the conserved arginine residue in the ParA-interacting motif of ParB and propose that rather than acting as an arginine finger, it interacts with negatively changed residues on ParA, likely promoting structural changes at its catalytic center required for ATP hydrolysis

We used Hydrogen/deuterium exchange mass spectrometry to show that ParB and nsDNA bind cooperatively to ParA and act synergistically to induce conformational changes in the catalytic site of ParA that correlate with the activation of its ATPase activity.

Moreover, we show that ParB clamps preferentially interact with ParA in their closed CTP-bound conformation ensuring that only partition complex-associated ParB molecules can effectively interact with nucleoid-bound ParA dimers.

We used an integrative structural approach combining AF modeling, X-ray crystallography, and NMR spectroscopy to map the interaction interfaces on both proteins. We found that the N-terminal ParA-binding motif of ParB binds at the ParA dimer interface, near its catalytic center.