Figure 1: Sequence analysis and the predicted structure of PfTatD.
From: The TatD-like DNase of Plasmodium is a virulence factor and a potential malaria vaccine candidate

(a) The TatD sequence alignment across various strains of Plasmodium and E. coli. The plasmodial TatD sequences contain a 24–26 AA signal peptide, whose cleavage site was between residues 26 and 27 in the P. falciparum or between 24 and 25 in other genera (blue box). A gap appeared in the predicted TatD DNase domain (yellow box) following a potent cell-binding residue (red box). The AAs that constitute the active site are indicated by red stars along the sequence. (b) The PfTatD 3D structure model was built using SWISS-MODEL. A template that contained 9 α-helices (green bands) and 8 β-pleated sheets (purple bands) in the secondary structure constituted a stable region. The yellow band indicates the gap in the TatD DNase domain. The red cylindrical bonds (red stars) indicate the conserved active site presented in a. (c) The schematic structural composition of the PfTatD domains. A 23-AA signal peptide site at the N terminus, followed by a 73-AA sequence gap (yellow rounded rectangle) that interrupted the TatD DNase domain, and AA residues from 224 to 362 indicated by the cerulean rounded rectangle.