Refaeli, Bosmat Giladi, Moshe Hiller, Reuben Khananshvili, Daniel Structure-Based Engineering of Lithium-Transport Capacity in an Archaeal Sodium–Calcium Exchanger Members of the Ca<sup>2+</sup>/cation exchanger superfamily (Ca<sup>2+</sup>/CA) share structural similarities (including highly conserved ion-coordinating residues) while exhibiting differential selectivity for Ca<sup>2+</sup>, Na<sup>+</sup>, H<sup>+</sup>, K<sup>+</sup>, and Li<sup>+</sup>. The archaeal Na<sup>+</sup>/Ca<sup>2+</sup> exchanger (NCX_Mj) and its mammalian orthologs are highly selective for Na<sup>+</sup>, whereas the mitochondrial ortholog (NCLX) can transport either Li<sup>+</sup> or Na<sup>+</sup> in exchange with Ca<sup>2+</sup>. Here, structure-based replacement of ion-coordinating residues in NCX_Mj resulted in a capacity for transporting either Na<sup>+</sup> or Li<sup>+</sup>, similar to the case for NCLX. This engineered protein may serve as a model for elucidating the mechanisms underlying ion selectivity and ion-coupled alternating access in NCX and similar proteins. Na;Li;protein;residue;mitochondrial ortholog;ion selectivity;exchanger;NCX;NCLX 2016-03-09
    https://acs.figshare.com/articles/journal_contribution/Structure_Based_Engineering_of_Lithium_Transport_Capacity_in_an_Archaeal_Sodium_Calcium_Exchanger/3102718
10.1021/acs.biochem.6b00119.s001