Figure 3
Ligand interactions and conformational changes of PfCCT(581–775) upon ligand binding. Close-up views of the substrate/product binding sites of PfCCT. (a) CDPCho-PfCCT structure, (b) CMP-PfCCT structure, (c) ChoP-PfCCT structure and (d) Cho-PfCCT structure. Ligand interaction residues are labelled and showed in stick representation. Interactions with the nucleotide and choline moieties of ligands are represented by black and orange dashed lines, respectively. (e) Conformational changes of active site residues Y626, Q636 and K663 in different ligand complexes of PfCCT(581–775). Binding of nucleotide ligands induces a shift of Q636 and Y626 from state 1 to state 2. The K663 residue sidechain is not rendered fully visible in the free enzyme as well as in Cho and CMP complexes.
