Structural highlights
Function
[AT1A1_RAT] This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Na,K-ATPase hydrolyzes ATP to drive the coupled extrusion and uptake of Na+ and K+ ions across the plasma membrane. Here, we report two high-resolution NMR structures of the 213-residue nucleotide-binding domain of rat alpha1 Na,K-ATPase, determined in the absence and the presence of ATP. The nucleotide binds in the anti conformation and shows a relative paucity of interactions with the protein, reflecting the low-affinity ATP-binding state. Binding of ATP induces substantial conformational changes in the binding pocket and in residues located in the hinge region connecting the N- and P-domains. Structural comparison with the Ca-ATPase stabilized by the inhibitor thapsigargin, E2(TG), and the model of the H-ATPase in the E1 form suggests that the observed changes may trigger the series of events necessary for the release of the K+ ions and/or disengagement of the A-domain, leading to the eventual transfer of the gamma-phosphate group to the invariant Asp369.
ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase.,Hilge M, Siegal G, Vuister GW, Guntert P, Gloor SM, Abrahams JP Nat Struct Biol. 2003 Jun;10(6):468-74. PMID:12730684[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hilge M, Siegal G, Vuister GW, Guntert P, Gloor SM, Abrahams JP. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase. Nat Struct Biol. 2003 Jun;10(6):468-74. PMID:12730684 doi:http://dx.doi.org/10.1038/nsb924
