Three‐dimensional structure of renal Na,K‐ATPase determined by electron microscopy of membrane crystals
- 22 July 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 187 (1) , 182-186
- https://doi.org/10.1016/0014-5793(85)81238-2
Abstract
The three-dimensional structure of Na,K-ATPase was determined by electron microscopy and image processing. Tilt series of negatively stained membrane crystals were recorded. The projections were analyzed by Fourier methods and the data combined to a 3-D model. The unit cell contains two rod-shaped stain-deficient regions interpreted as αβ-protomers of Na,K-ATPase. The rods are related by dyad axes oriented perpendicular to the membrane. Outside the lipid bilayer the rods contact different protein units on the two sides of the membraneKeywords
This publication has 12 references indexed in Scilit:
- Structural organization of (Na+ + K+)-ATPase in purified membranes.The Journal of cell biology, 1984
- Structure of (Na+,K+)-ATPase as revealed by electron microscopy and image processing.The Journal of cell biology, 1984
- The “EM” program systemUltramicroscopy, 1982
- Exclusive labeling of the extracytoplasmic surface of sodium and potassium ion activated adenosine triphosphatase and a determination of the distribution of surface area across the bilayerBiochemistry, 1982
- Crystallization patterns of membrane-bound (Na+ + K+)-ATPaseBiochimica et Biophysica Acta (BBA) - Biomembranes, 1982
- Three-dimensional structure of cytochrome c oxidase vesicle crystals in negative stainJournal of Molecular Biology, 1982
- Three-dimensional structure determination by electron microscopy of two-dimensional crystalsProgress in Biophysics and Molecular Biology, 1982
- Formation of two‐dimensional crystals in pure membrane‐bound Na+,K+‐ATPaseFEBS Letters, 1981
- Three-dimensional model of purple membrane obtained by electron microscopyNature, 1975
- Purification and characterization of (Na+ + K+)-ATPase IV. Estimation of the purity and of the molecular weight and polypeptide content per enzyme unit in preparations from the outer medulla of rabbit kidneyBiochimica et Biophysica Acta (BBA) - Biomembranes, 1974