Extended Data Fig. 3: Binding of the leader peptide activates PsnB.
From: Molecular mechanism underlying substrate recognition of the peptide macrocyclase PsnB
a, LP (PsnA214-24) enhances the affinity of the CP (PsnA228-38) to PsnB. Fraction bound of Fl_CP (0.1 µM) to PsnB (50 µM) was determined by fluorescence anisotropy. b, LP enhances the ATPase activity of PsnB. Basal ATP consumption rate of PsnB was 0.14 min-1enz-1, whereas the addition of 200 μM LP increased the ATP consumption rate to 0.89 min-1enz-1. P value < 0.01 by two-sided Student’s t-test. c, Fluorescence anisotropy of Fl_LP (0.1 µM) to wild-type PsnB or leader-fused PsnB (LP_PsnB). Data are presented as dot plots with mean ± 1 SD (n = 3 independent experiments; a-c) and fitted to a hyperbolic equation (c).
