Allosteric modulation of Plasmodium falciparum Isoleucyl tRNA synthetase by South African natural compounds
Fig 9
A) Holo average BC values mapped to structure, with largest BC residues (top 5%: 45 residues) shown as spheres on the structure, sticks in the enlarged window, and shown in a bar plot. AMP and Ile ligands are coloured magenta and green, respectively. A major allosteric pathway is seen, spanning the entire length of the enzyme, connecting the junctional domain to the active site and then the editing domain. B) Delta BC heatmap. The blue colour indicates a decrease from the holo-averaged protein, while the red colour indicates an increase. Residues per system with the largest change in BC (top/bottom 3% delta: 54 residues) relative to holo are shown with an “x”. Residues in the heatmaps not shown with an “x” are not in the top/bottom 3% in their respective system; these are included for comparison purposes. SANC ligand-induced BC changes of active site, zinc finger domain, and editing domain may be linked to enzyme functional change shown by the decreased binding affinity of AMP.