TY - JOUR
T1 - The enlightening encounter between structure and function in the NhaA Na+-H+ antiporter
AU - Padan, Etana
PY - 2008/9
Y1 - 2008/9
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=50449090660&partnerID=8YFLogxK
U2 - 10.1016/j.tibs.2008.06.007
DO - 10.1016/j.tibs.2008.06.007
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C2 - 18707888
AN - SCOPUS:50449090660
SN - 0968-0004
VL - 33
SP - 435
EP - 443
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 9
ER -