Fig. 1: Structure of ScIleRS with bound ligands.
From: Inhibitory mechanism of reveromycin A at the tRNA binding site of a class I synthetase
a Chemical structures of reveromycin A (RM-A) and the intermediate product Ile-AMP. b Overview of the ScIleRS ∙ RM-A ∙ Ile-AMP complex structure determined at a resolution of 1.9 Å. The residue numbers in the colour-coded diagram indicate domain boundaries. RM-A and Ile-AMP are shown in spherical models. The colour schemes for RM-A (green) and Ile-AMP (salmon) are the same throughout the manuscript. The α-helices forming the binding pocket of RM-A are labelled. c An annealed omit electron density map of RM-A and intermediate Ile-AMP calculated with Fourier coefficients Fo - Fc and contoured at 2.5 σ. RM-A and Ile-AMP co-bind in the aminoacylation pocket of the catalytic domain.
