Molecular imaging of Na+,K(+)-ATPase in purified kidney membranes.
Ion channels and pumps in cell membranes consist of multiple transmembrane segments that are thought to be critical for transport of ions. Channel structures constituted by these transmembrane segments are characteristic of ion channels, whereas such structures have not been identified in ion pumps until now. By applying atomic force microscopy on Na+,K(+)-ATPase molecules in canine kidney membranes under tapping mode, we identified a hollow in the protein with a characteristic internal diameter of 6-20 A and an external diameter of 20-55 A depending upon treatment conditions. This hollow may be interpreted as a channel-like conformation of Na+,K(+)-ATPase. In the regions where the proteins were absent, lipid head structures with 2 A width and 6 A length were imaged in an orthorhombic lattice.
Department of Medical Biochemistry, Ohio State University, Columbus 43210.
J K
JK
Paul
S R
SR
Nettikadan
M
M
Ganjeizadeh
M
M
Yamaguchi
K
K
Takeyasu
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology* / Q000648:ultrastructure; D004285:Dogs; D007091:Image Processing, Computer-Assisted; D007679:Kidney Medulla / Q000201:enzymology* / Q000648:ultrastructure; D008853:Microscopy / Q000379:methods*; D008854:Microscopy, Electron; D011487:Protein Conformation; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry / Q000648:ultrastructure*
D000254:Sodium-Potassium-Exchanging ATPase