Fig. 3
From: Trapping of the transport-segment DNA by the ATPase domains of a type II topoisomerase
X-ray crystal structure of ParE44 with side-bound 5′-GCGCGC-3′ duplex DNA and AMP-PNP. a, b, c Front, side and bottom views of the complex and d residues that interact with the DNA and were targeted for mutagenesis (underscored). The ParE44 protein forms a closed dimer with two molecules of DNA bound as a regular B-form helix but on the outside of the protein rather than in the hole. N-terminal ParE domains are shown in cartoon mode in light blue and cyan, bound AMP-PNP molecules are in red and DNA is in mauve/yellow for backbone/bases, respectively
