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

Rongxin Nie, Steven Stark, Jindrich Symersky, Ronald S. Kaplan and Min Lu ()
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Rongxin Nie: Rosalind Franklin University of Medicine and Science
Steven Stark: Rosalind Franklin University of Medicine and Science
Jindrich Symersky: Rosalind Franklin University of Medicine and Science
Ronald S. Kaplan: Rosalind Franklin University of Medicine and Science
Min Lu: Rosalind Franklin University of Medicine and Science

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: Abstract 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.

Date: 2017
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DOI: 10.1038/ncomms15009

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