Abstract
The aspartate transporter GltPH is an integral membrane protein that catalyses the movement of aspartate across lipid bilayers. GltPH utilises established ion gradients, transporting two sodium ions with each aspartate molecule. Previous studies have shown that the ion binding sites demonstrate selectivity for Na+ over both Li+ and K+ (Na+ > Li+ > K+) [1]. The sodium binding motif is similar to that of another sodium dependent leucine transporter, LeuT. Computational studies have attributed different mechanisms to ion selectivity in each of the two sodium binding sites in LeuT [2].
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