Fig. 6: Conformational changes upon ATP binding.
From: Structure and efflux mechanism of the yeast pleiotropic drug resistance transporter Pdr5
The two panels depict the molecular structure model of inward-facing (a) and outward-facing (b) conformations of Pdr5 in cartoon representation, and as a solvent-excluded surface with its cross-section. a Shown is the Pdr5 in the post-hydrolytic state, with ADP present in the catalytic site (ADP-Pdr5) and the transport channel open onto the cytoplasmic side. The position of the substrate entrance cavity is indicated. b The Pdr5 in the vanadate-trapped, outward-facing state is depicted. The exit channel for the substrate, which opens onto the extracellular side, is indicated as well. Abbreviations: ECD, extracellular domain; NBD, nucleotide-binding domain; TMD, transmembrane domain.
