On a daily basis, we observe the deterioration in the performance of man-made machines following extended use.
However, it is unknown whether biological machines undergo the same “wear and tear” associated with constant activity.
Here we show that a membrane-bound ATPase is not adversely affected by constant activity. On the contrary, it benefits from it. We find that constant activity maintains the structural and functional integrity of the E. coli ABC transporter BtuCD. Remarkably, with respects to its ability to interact with its cognate receptor, the constantly active transporter even out-performs the freshly prepared one. None of the reaction intermediates mimic the full beneficial effects conveyed by completing the full cycle of ATP hydrolysis. In other words, to gain full advantage the ATPase must hydrolyze ATP.
We discuss here the implications of our findings with respect to protein stability and folding, and possible physiological implications.
