Fig. 4: OB covalently modifies the engineered Lys462.
From: Tyrosine-targeted covalent inhibition of a tRNA synthetase aided by zinc ion
a Diagram of the Tm value of ThrRS_WT and ThrRS_Y462K in the presence or absence of OB and 36j. Evaluations were carried out in four repeats, and error bars indicate the respective standard deviation (n = 4, mean value ± SD). All data points are shown in small circles. Numerical Data can be found in Supplementary Data 1. b Superimposition of the structures of ThrRS_WT-OB and ThrRS_Y462K-OB. The r.m.s.d is 0.421 Å over 322 Cα atoms. c The catalytic center of ThrRS_Y462K bound to OB. The ε-amino group of Lys462 (presented as green sticks) forms an amide bond with OB (presented as orange sticks). The linkage atoms of the original 4-membered ring in OB are indicated by red stars. Interacting residues are shown as sticks. The 2Fo-Fc electron density of Lys462-OB (contoured at 1.0 σ) is shown as a transparent surface. d Close-up view of residues coordinating with a Zn2+ ion. The 2Fo-Fc electron density of the involved residues (contoured at 1.0 σ) is shown as a transparent surface.
