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Significance Na+ /Ca2+ exchangers (NCXs) have a key role in the homeostasis of cellular Ca2+ and consequently are implicated in diverse human-health disorders, including neurodegenerative and cardiovascular diseases. A detailed understanding of the molecular mechanisms of these membrane proteins is therefore of interest from fundamental and biomedical standpoints. Here, we establish the structural mechanism of Na+ recognition in a prokaryotic NCX homolog, using atomistic molecular-dynamics simulations based on recently reported crystallographic data, as well as experimental transport assays of wild-type and mutagenized exchangers. The results have general implications pertaining to the ion exchange stoichiometry and electrogenicity of the Na+ /Ca2+ transport cycle across the NCX family, and provide the basis for future investigations of the conformational mechanism of these important transporters.

Sodium recognition by the Na + /Ca 2+ exchanger in the outward-facing conformation

Sodium recognition by the Na ⁺ /Ca ²⁺ exchanger in the outward-facing conformation