Functional role of a structural water in the elevator domain of dicarboxylate transporter VcINDY

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ID: 321240
2026
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Abstract
Abstract The divalent anion sodium symporter (DASS) family mediates the uptake of Krebs cycle intermediates and sulfate, and influences adiposity, insulin resistance, and metabolism in mammals. While Na+:substrate stoichiometry is known for several DASS transporters, the location of key Na+ binding sites remains elusive; important information for understanding the mechanism. In VcINDY, a bacterial DASS protein, we visualized a non-protein cryo-EM density in the middle of the transport domain. Its size and coordination suggest it may represent either a third Na+ ion or a structural water molecule. Using a combination of in vitro binding and transport assays, cryo-EM structural determination and molecular dynamic simulations, we show that the density is not a Na+ ion. Instead, the data indicate that the density likely represents a structural water molecule critical for transport domain integrity. Sequence and structural similarities suggest this feature may be conserved across human DASS transporters such as NaCT and NaDC3.
Reference Key
openalex_W7168738806 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Andrew Daab, Yan Li, Jennifer J. Marden, Jinmei Song, David B. Sauer, Da‐Neng Wang, Christopher Mulligan
Journal PNAS nexus
Year 2026
DOI
10.1093/pnasnexus/pgag242
URL
https://doi.org/10.1093/pnasnexus/pgag242
Keywords Keywords not found

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