Crystal structures of Mtb RNAP bound to
rifampin (left), Mtb RNAP bound to an AAP (center), and Mtb RNAP bound to both
rifampin and an AAP (right) show that
rifampin and the AAP interact with non-overlapping binding sites
on Mtb RNAP and, as a result, can bind simultaneously to Mtb RNAP.
Intensive efforts also have been underway to develop new, non
rifampin - related Mtb RNAP inhibitors that function through binding sites
on Mtb RNAP that do not overlap the
rifampin binding site and that thus can kill
rifampin - resistant TB bacteria.