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Integral membrane proteins of the divalent anion/Na +  symporter (DASS) family translocate dicarboxylate, tricarboxylate or sulphate across cell membranes, typically by utilizing the preexisting Na +  gradient. The molecular determinants for substrate recognition by DASS remain obscure, largely owing to the absence of any substrate-bound DASS structure. Here we present 2.8-Å resolution X-ray structures of VcINDY, a DASS from  Vibrio cholerae  that catalyses the co-transport of Na +  and succinate. These structures portray the Na + -bound VcINDY in complexes with succinate and citrate, elucidating the binding sites for substrate and two Na +  ions. Furthermore, we report the structures of a humanized variant of VcINDY in complexes with succinate and citrate, which predict how a human citrate-transporting DASS may interact with its bound substrate. Our findings provide insights into metabolite transport by DASS, establishing a molecular basis for future studies on the regulation of this transport process.

Structure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variant