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. Author manuscript; available in PMC: 2020 Mar 1.
Published in final edited form as: Nat Struct Mol Biol. 2019 Aug 26;26(9):792–801. doi: 10.1038/s41594-019-0280-4

Fig. 3. Consensus thermodynamic model for transport by ABC exporters.

Fig. 3.

Vertically aligned (a) energy diagram and (b) conformational state schematics for transport cycle of type I ABC exporters. The resting state (1) is inward open. Substrate and ATP binding promotes transition through substrate-bound occluded states (2, 3), to a locally stable outward-open state (4), with an ATP-dependent NBD dimer. Substrate-bound transporters have a lower transition energy (red box), accounting for the observed substrate stimulation. After substrate release (5), ATP hydrolysis destabilizes the NBD dimer and outward-open state, leading the transporter to transition through an occluded state (6) and ending at the inward-open state (7) concomitant with release nucleotide, resetting for another round of transport.