Two-dimensional crystalline arrays of Na,K-ATPase with new subunit interactions induced by cobalt-tetrammine-ATP

J Ultrastruct Mol Struct Res. 1989 Dec;102(3):189-95. doi: 10.1016/0889-1605(89)90013-x.

Abstract

Purified membrane-bound Na,K-ATPase incubated with cobalt-tetrammine-ATP [Co(NH3)4ATP], which is a stable MgATP complex analog, shows two new types of membrane crystals, a new p21 form and a p4 form. The building blocks of the crystalline arrays correspond to (alpha beta)2 dimers of the enzyme protein suggesting that alpha-alpha interaction may be important in the pumping process.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / analogs & derivatives*
  • Animals
  • Cobalt*
  • Crystallization*
  • In Vitro Techniques
  • Membrane Proteins / isolation & purification*
  • Membrane Proteins / ultrastructure
  • Microscopy, Electron
  • Organometallic Compounds*
  • Sodium-Potassium-Exchanging ATPase / isolation & purification*
  • Swine

Substances

  • Membrane Proteins
  • Organometallic Compounds
  • Cobalt
  • tetraamminecobalt(III)ATP
  • Adenosine Triphosphate
  • Sodium-Potassium-Exchanging ATPase