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

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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)

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.

Suggested Citation

  • Rongxin Nie & Steven Stark & Jindrich Symersky & Ronald S. Kaplan & Min Lu, 2017. "Structure and function of the divalent anion/Na+ symporter from Vibrio cholerae and a humanized variant," Nature Communications, Nature, vol. 8(1), pages 1-10, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15009
    DOI: 10.1038/ncomms15009
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    Cited by:

    1. James S. Davies & Michael J. Currie & Rachel A. North & Mariafrancesca Scalise & Joshua D. Wright & Jack M. Copping & Daniela M. Remus & Ashutosh Gulati & Dustin R. Morado & Sam A. Jamieson & Michael , 2023. "Structure and mechanism of a tripartite ATP-independent periplasmic TRAP transporter," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Martin F. Peter & Jan A. Ruland & Peer Depping & Niels Schneberger & Emmanuele Severi & Jonas Moecking & Karl Gatterdam & Sarah Tindall & Alexandre Durand & Veronika Heinz & Jan Peter Siebrasse & Paul, 2022. "Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    3. David B. Sauer & Jennifer J. Marden & Joseph C. Sudar & Jinmei Song & Christopher Mulligan & Da-Neng Wang, 2022. "Structural basis of ion – substrate coupling in the Na+-dependent dicarboxylate transporter VcINDY," Nature Communications, Nature, vol. 13(1), pages 1-9, December.

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