Extended Data Fig. 9: IstA interaction with the donor DNA.
From: Molecular basis for transposase activation by a dedicated AAA+ ATPase
![Extended Data Fig. 9](https://cdn.statically.io/img/media.springernature.com/full/springer-static/esm/art%3A10.1038%2Fs41586-024-07550-6/MediaObjects/41586_2024_7550_Fig15_ESM.jpg)
a, The two catalytic monomers of the IstA tetramer (lower chains, green) interact with the R1 repeat or a TIR while the upper structural subunits (pink) engage the R2 sequence. Only two IstA molecules and one TIR duplex are depicted, the rest of the complex is shown as a transparent surface for clarity. The base pair separating both repeats is colored in red. b, The β-barrel of the upper (pink) and lower (green) IstA subunits use similar areas to interact with other subunits of the transposase and the donor DNA, and IstB, respectively. The β-barrel of the upper monomers contains an extra, ordered alpha-helix (Phe361-Ala373) at the C-terminus that contacts the 5’ overhang (non-transferred strand) of the donor DNA.