Figure 4
Structural comparison of PfCCT and RnCCT catalytic domain in complex with CDPCho. (a) Sequence alignment of PfCCT(581–775) and the corresponding region of RnCCT. Strictly conserved residues are indicated as white letters on red background and similar residues as red letters on white background. The secondary structure elements are added above the sequence. We also noted by a star all residues mentioned in the text, including active site residues and non-conserved residues. Residue numbers are noted where the lysine-rich specific loop (720–737) has been removed. The layout was created by ESPript 3.057. (b) Structural alignment of PfCCT (violet) and RnCCT (PDB: 3HL4) (light orange) monomers complexed with CDPCho. CDPCho is coloured by atoms with green and deep blue carbons in PfCCT and RnCCT complex structures, respectively. Dashed circle designates the core region which is highly similar in PfCCT and RnCCT structures. (c) Close-up view of the CDPCho interaction network. (d) Superposition of 3 non-conserved active site residues between PfCCT and RnCCT and displacement of the signature sequence fragment (PfCCT: 759VSTT762; RnCCT: 200ISTS203) located at the border of loop L6 and helix αE. Residues V625, Y626 and Q636 in PfCCT correspond to I84, F85 and A95 in RnCCT, respectively. Distances between atoms showed by dashed line are in Å.
