Two-dimensional crystalline arrays of Na,K-ATPase with new subunit interactions induced by cobalt-tetrammine-ATP.
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.
Skriver
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E
Department of Cell Biology, University of Aarhus, Denmark.
Maunsbach
A B
AB
Hebert
H
H
Scheiner-Bobis
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G
Schoner
W
W
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives*; D000818:Animals; D003035:Cobalt; D003460:Crystallization; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000302:isolation & purification* / Q000648:ultrastructure; D008854:Microscopy, Electron; D009942:Organometallic Compounds; D000254:Sodium-Potassium-Exchanging ATPase / Q000302:isolation & purification*; D013552:Swine
D008565:Membrane Proteins; D009942:Organometallic Compounds; D003035:Cobalt; C020511:tetraamminecobalt(III)ATP; D000255:Adenosine Triphosphate; D000254:Sodium-Potassium-Exchanging ATPase