Figure 1

Molecular architecture of Tgf2 transposase.

(a) The domains of full length Tgf2 transposase (L-Tgf2TPase) (686 aa). (b) The secondary structure of the N-terminal zinc finger domain. Two conserved cysteine (C) and two conserved histidine (H) residues are indicated with dark triangles. The α-helices (green) and β-strands (yellow) are also shown. (c) The three-dimensional model of the N-terminal zinc finger domain, which consists of an α-helix (red), two antiparallel β-sheets (yellow) and a motif usually used for DNA-binding (green). Two histidine (H₁₀₆, H₁₁₁) and two cysteine (C₈₃, C₈₆) residues (blue) form a cave that can bind a zinc ion. (d) The homology model of the full length Tgf2 transposase. α-helices and β-strands are colored in red and yellow respectively. Residues of the DDE (D₂₂₈, D₂₉₅ and E₆₄₈) active site triads are labeled. (e) Close-up view of the DDE active site.