Fig. 4: Conformational dynamics in the JtNorQ^WBNorD dataset.

a Models of states 2–4 are superimposed on the N-terminal domain of NorD (purple) and shown as side views in the top row, with all NorQ subunits represented as transparent surfaces, except for the ATP-loaded seam subunit (A, A*), which is shown as tube helices. A* marks the new seam subunit after ATP binding and reaching up of the bottom seam subunit. The bottom row displays the isolated NorD domains from the above complex in the same viewing direction. ATP molecules shown in red space fill representation. NorD VWA domain is shown as hot pink tube helices with the finger in red. b Superposition of the NorD VWA domain, illustrating the rotation between the finger and VWA domains between states 1–3 and state 4. CT denotes the NorD C-terminus. c Arrangement of the NorQ postS1 loops (blue) and the NorD VWA domain (pink, finger in red) in states 1–3 (left) and state 4 (right) of JtNorQ^WBNorD, viewed from the top of the complex. The N-terminal domain of NorD can bind to either the C or B subunit of NorQ. The orientation of the C-terminus of NorD towards the postS1 loop differs between states 1–3 and state 4 (central panel). d Overlay of postS1 loops in NorQ, chains A, B, C and E, of state 1 (top) and state 4 (bottom). The postS1 loop of chain E adopts a conformation as observed in ATP bound subunits when bound to the NorD C-terminus (state 1) but changes conformation when the NorD C-terminus is not bound (state 4). e Hydrophobic interactions in the NorQ pore of PdNorQ^WB/NorD^VWA and JtNorQ^WB/NorD. The postS1 loops of NorQ subunits are shown as surface coloured by hydrophobicity. NorD model is shown as tubes and planks. The NorD C-terminus (CT) and the interacting NorQ protomers are labelled. f The postS1 loops of NorD-interacting protomers are shown and individual amino acids labelled. NorD is displayed as surface representation coloured by hydrophobicity (yellow: hydrophobic, cyan: hydrophilic).