Abstract
The divalent anion sodium symporter (DASS) family of plasma membrane transporters import di- and tricarboxylates essential to metabolic signaling and cellular regulation. While DASS proteins transport substrates via an elevator mechanism, previous structures were of only a single DASS cotransporter protein in a substrate-bound, inward-facing state. We have determined cryo-EM and X-ray structures of multiple DASS proteins in several different states, including three hitherto unseen states. Comparison of these structures reveal how the transport domain translates and rotates within the framework of the scaffold domain through the transport cycle. Additionally, we propose that DASS transporters ensure substrate coupling by a charge-compensation mechanism, and by structural changes upon substrate release.
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