1MO8: ATPase
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
ID 4531050
Author(s) Hilge, M; Siegal, G; Vuister, GW; Guentert, P; Gloor, SM; Abrahams, JP
Author(s) at UniBasel Abrahams, Jan Pieter
Year 2003
Title 1MO8: ATPase
Journal Worldwide Protein Data Bank
Pages / Article-Number 1MO8
Keywords Hydrolase
Mesh terms Science & TechnologyLife Sciences & BiomedicineBiochemistry & Molecular BiologyBiochemistry & Molecular Biology

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.

Full Text on edoc
Digital Object Identifier DOI 10.2210/pdb1mo8/pdb
ISI-Number DRCI:DATA2012136001725619
Document type (ISI) Data set

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