Crystal structure of the plasma membrane proton pump
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Crystal structure of the plasma membrane proton pump. / Pedersen, Bjørn P.; Buch-Pedersen, Morten Jeppe; Morth, J. Preben; Palmgren, Michael Gjedde; Nissen, Poul.
In: Nature, Vol. 450, No. 7172, 2007, p. 1111-1115.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - Crystal structure of the plasma membrane proton pump
AU - Pedersen, Bjørn P.
AU - Buch-Pedersen, Morten Jeppe
AU - Morth, J. Preben
AU - Palmgren, Michael Gjedde
AU - Nissen, Poul
PY - 2007
Y1 - 2007
N2 - A prerequisite for life is the ability to maintain electrochemical imbalances across biomembranes. In all eukaryotes the plasma membrane potential and secondary transport systems are energized by the activity of P-type ATPase membrane proteins: H1-ATPase (the proton pump) in plants and fungi1-3, and Na1,K1-ATPase (the sodium-potassium pump) in animals4. The name P-type derives from the fact that these proteins exploit a phosphorylated reaction cycle intermediate of ATP hydrolysis5.The plasma membrane proton pumps belong to the type III P-type ATPase subfamily, whereas Na1,K1-ATPase and Ca21- ATPase are type II6. Electron microscopy has revealed the overall shape of proton pumps7, however, an atomic structure has been lacking. Here we present the first structure of a P-type proton pump determined by X-ray crystallography. Ten transmembrane helices and three cytoplasmic domains define the functional unit of ATP-coupled proton transport across the plasma membrane, and the structure is locked in a functional state not previously observed in P-type ATPases. The transmembrane domain reveals a large cavity, which is likely to be filled with water, located near the middle of the membrane plane where it is lined by conserved hydrophilic and charged residues. Proton transport against a high membrane potential is readily explained by this structural arrangement.
AB - A prerequisite for life is the ability to maintain electrochemical imbalances across biomembranes. In all eukaryotes the plasma membrane potential and secondary transport systems are energized by the activity of P-type ATPase membrane proteins: H1-ATPase (the proton pump) in plants and fungi1-3, and Na1,K1-ATPase (the sodium-potassium pump) in animals4. The name P-type derives from the fact that these proteins exploit a phosphorylated reaction cycle intermediate of ATP hydrolysis5.The plasma membrane proton pumps belong to the type III P-type ATPase subfamily, whereas Na1,K1-ATPase and Ca21- ATPase are type II6. Electron microscopy has revealed the overall shape of proton pumps7, however, an atomic structure has been lacking. Here we present the first structure of a P-type proton pump determined by X-ray crystallography. Ten transmembrane helices and three cytoplasmic domains define the functional unit of ATP-coupled proton transport across the plasma membrane, and the structure is locked in a functional state not previously observed in P-type ATPases. The transmembrane domain reveals a large cavity, which is likely to be filled with water, located near the middle of the membrane plane where it is lined by conserved hydrophilic and charged residues. Proton transport against a high membrane potential is readily explained by this structural arrangement.
U2 - 10.1038/nature06417
DO - 10.1038/nature06417
M3 - Journal article
C2 - 18075595
VL - 450
SP - 1111
EP - 1115
JO - Nature
JF - Nature
SN - 0028-0836
IS - 7172
ER -
ID: 8098318