Short answers, pulled from the story.
MinD is one of three proteins encoded by the minB operon and a member of the ParA family of ATPases. It is a peripheral membrane ATPase that generates pole to pole oscillations before bacterial cell division to specify the midzone of the cell, and it is involved in plasmid partitioning.
MinD specifies the midzone by oscillating from pole to pole prior to cell division. Live-cell imaging by Raskin and de Boer using GFP fusion proteins showed that MinC and MinD rapidly oscillate between the two poles in a non-static manner rather than forming a stable cap.
The ATPase activity of MinD is activated by MinE in the presence of phospholipids. Membrane binding is thought to induce a conformational change that makes MinD susceptible to MinE activation, and its activity also depends on local MinD concentration.
In vitro studies on a two-dimensional supporting lipid bilayer showed that MinD forms a membrane-bound carpet in MinE mutants. Re-adding MinE made the system unstable and dynamic, and repeated attachment and detachment produced standing waves with a focused wave-front, demonstrating the Min system's ability to self-organize.
Single molecule dynamics revealed that MinD dimerizes while membrane-bound, creating a stronger membrane association at the rear of the standing wave and a diffusivity gradient. This diffusivity gradient explains the focused bands of fluorescence observed in the standing wave studies.
MinD belongs to the ParA family of ATPases. It is also one of three proteins encoded by the minB operon and acts as a peripheral membrane ATPase involved in plasmid partitioning.