Fig. 7
Proposed mechanism for the allosteric regulation of ToxTEPI dimerization by UFAs. Left: In the UFA-bound state, hydrophobic contacts between the UFA, Leu61 and L114, trap ToxT in a tense state in which the conformation of helix α3 precludes dimerization. Right: Release of UFA from ToxT relaxes helices α2 and α3, which are then able to adopt a conformation allowing dimerization on DNA.
