Extended Data Fig. 10: NicA2 wildtype and v321 titrations with NMM.
From: Directed evolution unlocks oxygen reactivity for a nicotine-degrading flavoenzyme
a, The signal for wildtype NicA2 Y342tmfF titrated with 0, 0.1, 0.5, and 2.5 mM NMM narrows with increasing NMM, indicating a more restricted sampling of local conformations. b, NicA2 v321 Y342tmfF titrated with NMM of the same concentrations as labeled, showing collapse into a single population. At increasing molar ratios, NMM yields a narrow major peak whose intensity increases with a concomitant decrease in the intensity of the apo- state peaks. Thus, NMM binding ‘pulls’ the distinct apo- state sub-ensembles that are in slow exchange into a single major conformation, one that presumably resembles the crystallized conformation of the NMM-bound NicA2 v321 complex. NMM, N-methylmyosmine.
