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. 2005 Apr 26;387(Pt 3):591–600. doi: 10.1042/BJ20041733

Figure 1. Amino acid sequence alignment and homology modelling of LdAdK.

Figure 1

(A) Alignment of LdAdK amino acid sequence with that of T. gondii (AAF01261), Babesia canis (CAA11263), Saccharomyces cerevisiae (P47143), human (AAA97893) and Chinese hamster ovary (CHO; AAA91648) AdK (numbers in parentheses indicate GenBank® accession numbers for respective proteins). Boxes indicate amino acid signature motifs distinctive of this family of proteins. The residues selected for site-directed mutagenesis, i.e. Gly-62, Arg-69, Arg-131 and Asp-299, of LdAdK are indicated in bold. The boxes represent amino acid sequence motifs that are distinctive of the PfkB family of carbohydrate kinases. (B) Homology model showing the overall structure of LdAdK with α-helices drawn as ribbons and β-strands as arrows. Spatial position of Ado (magenta), ATP (yellow), Gly-62 (cyan), Arg-69 (red), Arg-131 (white) and Asp-299 (pink) are shown in space-fill mode. (C) Zoomed picture of the active-site residues, with inter-atomic distances shown by broken lines.