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Control by Na/H antiporters of sodium/proton concentration and cell volume is crucial for the viability of all cells. Adaptation to high salinity and/or extreme pH in plants and bacteria or in human heart muscles requires the action of Na/H antiporters. Their activity is tightly controlled by pH. We determined the first crystal structure of a member of this family of secondary transporters, namely the structure of NhaA [1]. The latter is the main antiporter of Escherichia coli and many enterobacteria. An iterative process of optimizing protein and crystal quality was pursued to permit structure determination. The protein has been crystallized at low pH, i.e. NhaA is present in its pH down-regulated conformation. A negatively charged ion funnel opens to the cytoplasm and ends in the middle of themembrane at the putative ion-binding site. There, a unique assembly of two pairs of short helices connected by crossed, extended chains creates a balanced electrostatic environment. Based on the structure and on previous biochemical and genetic data, a working model for the pH-regulated ion translocation has been suggested. Binding of charged substrates causes electric imbalance inducingmovements, which allow for a rapid alternating access mechanism. This ion exchange machinery is regulated by a conformational change elicited by a pH signal perceived at the cytoplasmic funnel entry.

Structure of the Na+/H+antiporter NhaA

Structure of the Na⁺/H⁺antiporter NhaA