A model-structure of a periplasm-facing state of the NhaA antiporter suggests the molecular underpinnings of pH-induced conformational changes.

Although the current conformation cannot account for the above mentioned accessibility of residues in TMs IV, V, X, and XI ( 16 , 51 – 53 , 55 ), it does suggest a clear trend of opening toward the assembly region from both sides of the membrane ( Fig. 3 ).

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