1MO8

ATPase

Summary for 1MO8

• Entry DOI: 10.2210/pdb1mo8/pdb
• Related: 1MO7
• NMR Information: BMRB: 5576
• Descriptor: Sodium/Potassium-Transporting ATPase alpha-1, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• Functional Keywords: six-stranded, twisted beta sheet, hydrolase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cell membrane; Multi-pass membrane protein: P06685
• Total number of polymer chains: 1
• Total formula weight: 24376.31

Authors

Hilge, M.,Siegal, G.,Vuister, G.W.,Guentert, P.,Gloor, S.M.,Abrahams, J.P. (deposition date: 2002-09-08, release date: 2003-06-10, Last modification date: 2024-05-22)

Primary citation

Hilge, M.,Siegal, G.,Vuister, G.W.,Guentert, P.,Gloor, S.M.,Abrahams, J.P.
ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase
Nat.Struct.Biol., 10:468-474, 2003

PubMed Abstract: 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.

PubMed: 12730684
DOI: 10.1038/nsb924

Experimental method

SOLUTION NMR