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3D Reconstruction of Na+, K+-ATpase from Tubular Crystals

Published online by Cambridge University Press:  02 July 2020

W. J. Rice
Affiliation:
Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University Medical Center, 540 First Ave. New York, NY 10016
H.S. Young
Affiliation:
Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University Medical Center, 540 First Ave. New York, NY 10016
D.W. Martin
Affiliation:
Division of Hematology, Department of Medicine, State University of New York at Stony Brook, New York11794-8151
J. R. Sachs
Affiliation:
Division of Hematology, Department of Medicine, State University of New York at Stony Brook, New York11794-8151
D.L. Stokes
Affiliation:
Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University Medical Center, 540 First Ave. New York, NY 10016
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Extract

The Na+,K+-ATPase is a transmembrane protein, located in the plasma membrane of virtually all animal cells, which controls Na+ and K+ gradients. It is a member of the P-type ATPase family of ion pumps, a group of enzymes which pump ions against a concentration gradient, forming a phosphorylated intermediate during the pumping cycle. For each mole of ATP hydrolysed, 3 Na + ions are moved out of the cell and 2 K+ ions are moved into the cell. Unlike most other members of this family, which have one subunit, Na+, K+-ATPase is a heterodimer of α and β subunits. The a subunit consists of 1020 amino acids and has been predicted to have 10 membrane-spanning a-helices as well as a large cytoplasmic headpiece which forms the ATP binding and phosphorylation site. The α subunit, 300 amino acids in length, has one membrane spanning helix and has most of its mass located on the extracellular side of the membrane.

Type
Electron Cryomicroscopy of Macromolecules
Copyright
Copyright © Microscopy Society of America

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References

1.Martin, D. W. and Sachs, J.R.Biochemistry 38 (1999) 7485.CrossRefGoogle Scholar
2.DeRosier, D. et al., J. Mol. Biol. 289 (1999) 159.CrossRefGoogle Scholar
3. This work was suported by NIH grants GM 56960 (DLS) and DK19185 (JRS). WJR is suported by a postdoctoral fellowship from the Human Frontier Science Program. HSY is supported by a Scientist Development grant from the American Heart Association, Heritage Affiliate.Google Scholar