Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 33, Issue 9, Pages 435-443Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2008.06.007
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Funding
- United States-Israel Binational Science Foundation [501/03-16.2]
- EDICT [EU FP 7]
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Na+-H+ antiporters are integral membrane proteins that exchange Na+ for H+ across the cytoplasmic membrane and many intracellular membranes. They are essential for Na+, pH, and volume homeostasis, which are processes crucial for cell viability. Accordingly, antiporters are important drug targets in humans and underlie salt resistance in plants. Many Na+-H+ antiporters are tightly regulated by pH. Escherichia coli NhaA, a prototype pH-regulated antiporter, exchanges 2H(+) for 1Na(+) (or Li+). The NhaA crystal structure has provided insight into the pH-regulated mechanism of antiporter action and revealed transmembrane segments, which are interrupted by extended mid-membrane chains that have since been found with variations in other ion-transport proteins. This novel structural fold creates a delicately balanced electrostatic environment in the middle of the membrane, which might be essential for ion binding and translocation.
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