Fig. 3: Structural comparison of different catalytic states of NgLeuRS. | Communications Biology

Fig. 3: Structural comparison of different catalytic states of NgLeuRS.

From: Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip

Fig. 3: Structural comparison of different catalytic states of NgLeuRS.

a Top, ribbon representation of the superposition of the ternary structure of NgLeuRS·ATP·leucinol (magenta) with NgLeuRS (slate). Bottom, superposition of the ternary structure of NgLeuRS·ATP·leucinol (magenta) with NgLeuRS·Leu-AMP (green). In both panels the aminoacylation domain, CP2, Zn2, ACBD and CTD of the NgLeuRS·ATP·leucinol structure are additionally shown as a surface representation. b Top panels, the relative position of the CP1 hairpin (cartoon backbone representation) to the L550-containing α-helix (cartoon and stick representation) in different catalytic states. Ligands are shown as sticks representations while the Mg2+ ion is shown as a gray sphere. Bottom, zoom of the L550 region. 2Fo-Fc electron density maps countered at 1.5 σ (gray mesh). c Comparison of the Ramachandran plot of L550 (green square) and H551 (red circle) in NgLeuRS/NgLeuRS·Leu-AMP and NgLeuRS·ATP·leucinol structures. d Polar interactions between E169 in the CP1 hairpin and surrounding protein residues in the NgLeuRS·ATP·leucinol complex. H-bonds are shown as black dashed lines.

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