Structure comparison of (a) GyrB43⋅ADP⋅P_i (magenta) and (b) GyrB43⋅ADP⋅BeF₃ (violet) with GyrB43⋅AMPPNP (shown as a dimer with yellow/grey colour with molecular dyad in black).

<p>The structures are superimposed on their ATPase domain (residues 20–220). The rotation axes for the domain reorientation of the transducer domain with respect to the ATPase domain are indicated. These form an angle of 21.5° and 14.5° with the molecular dyad for GyrB⋅ADP⋅P_i and GyrB⋅ADP⋅BeF₃, respectively. The insets show the QTK loop of the transducer domain that is rotated relative to the ATPase domain in response to the nucleotide state (dashed lines); Q: Q335, K: K337. (c) Stereoview of the overlay of the three aforementioned structures.