Fig. 2: The unpaired residue A36-mediated dynamic pivoting of Helices E and B3 is crucial for the efficient recognition by TyrRS.
From: Structural insights into dynamics of the BMV TLS aminoacylation
a Schematic representation of the unbound TLS structure. The left panel shows the cryo-EM map and atomic model of the unbound TLS, while the right panel illustrates its secondary structure. b Superimposed model and map of TLS-TyrRS in the pre-1a state. c Domain organization of a single TyrRS subunit. d Comparison of the unbound TLS structure (left, transparent with colors) and the bound TLS structure (right, solid colors), demonstrating conformational changes upon binding. e Overlay of the B1, B3, and E helices in the two states of TLS, along with a magnified view of the detailed alignment at residue A36 (transparent colors for unbound TLS, solid colors for bound TLS). Helix B1 remains almost unchanged, while A36, located at the junction of helices B1 and B3, shows an 8-Å displacement in the phosphate backbone. A cartoon schematic (right) illustrates how A36 mediates the dynamic rearrangement of helices E and B3. f In vitro aminoacylation assay to confirm the importance of A36. Data are shown as the mean ± SD (n = 3 independent experiments). Source data are provided as a Source Data file.
