NDLI: Mutation of Gly-94 in transmembrane segment M1 of $Na^{+},K^{+}-ATPase$ interferes with $Na^{+}$ and $K^{+}$ binding in $E_{2}P$ conformation

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Mutation of Gly-94 in transmembrane segment M1 of $Na^{+},K^{+}-ATPase$ interferes with $Na^{+}$ and $K^{+}$ binding in $E_{2}P$ conformation

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Mutation of Gly-94 in transmembrane segment M1 of $Na^{+},K^{+}-ATPase$ interferes with $Na^{+}$ and $K^{+}$ binding in $E_{2}P$ conformation

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Andersen, Jens Peter Einholm, Anja Pernille Toustrup-jensen, Mads Vilsen, Bente
Description	Author Affiliation: Einholm AP ( Department of Physiology, Institute of Physiology and Biophysics, University of Aarhus, DK-8000 Aarhus C, Denmark.);
Abstract	The importance of Gly-93 and Gly-94 in transmembrane segment M1 of the Na+,K+-ATPase for interaction with Na+ and K+ was demonstrated by functional analysis of mutants Gly-93-Ala and Gly-94-Ala. In the crystal structures of the Ca2+-ATPase, the corresponding residues, Asp-59 and Leu-60, are located exactly where M1 bends. Rapid kinetic measurements of K+-induced dephosphorylation allowed determination of the affinity of the E2P phosphoenzyme intermediate for K+. In Gly-94-Ala, the K+ affinity was reduced 9-fold, i.e., to the same extent as seen for mutation of the cation-binding residue Glu-329. Furthermore, Gly-94-Ala showed strongly reduced sensitivity of the E1P-E2P equilibrium to Na+, with accumulation of E2P even at 600 mM Na+, indicating that interaction of E2P with extracellular Na+ is impaired. On the contrary, in Gly-93-Ala, the affinity for K+ was slightly increased, and the E1P-E2P equilibrium was displaced in favor of E1P. In both mutants, the affinity of the cytoplasmically facing sites of E1 for Na+ was reduced, but this effect was relatively small compared with the effects seen for E2P in Gly-94-Ala. Comparison with Ca2+-ATPase mutagenesis data suggests that the role of M1 in binding of the transported ions is universal among P-type ATPases, despite the low sequence homology in this region. Structural modeling of Na+,K+-ATPase mutant Gly-94-Ala on the basis of the Ca2+-ATPase crystal structures indicates that the alanine side chain comes close to Ile-287 of M3, particularly in E2P, thus resulting in a steric clash that may explain the present observations.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	32
Volume Number	102
Language	English
Publisher	National Academy of Sciences
Publisher Date	2005-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Models, Molecular Potassium Metabolism Sodium-Potassium-Exchanging ATPase Genetics Sodium Adenosine Triphosphate Amino Acid Sequence Animals COS Cells Cercopithecus Aethiops DNA, Complementary Molecular Sequence Data Mutagenesis, Site-Directed Ouabain Phosphorylation Protein Binding Protein Conformation Protein Structure, Tertiary Sequence Alignment Comparative Study Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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