NDLI: Neutralization of the Charge on $Asp^{369}$ of $Na^{+},K^{+}-ATPase$ Triggers $E_{1}$ ↔ $E_{2}$ Conformational Changes

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Neutralization of the Charge on $Asp^{369}$ of $Na^{+},K^{+}-ATPase$ Triggers $E_{1}$ ↔ $E_{2}$ Conformational Changes

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Neutralization of the Charge on $Asp^{369}$ of $Na^{+},K^{+}-ATPase$ Triggers $E_{1}$ ↔ $E_{2}$ Conformational Changes

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Haviv, Haim Belogus, Talya Karlish, Steven J. D.
Description	Author Affiliation: Belogus T ( Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.)
Abstract	This work investigates the role of charge of the phosphorylated aspartate, Asp(369), of Na(+),K(+)-ATPase on E(1) <--> E(2) conformational changes. Wild type (porcine alpha(1)/His(10)-beta(1)), D369N/D369A/D369E, and T212A mutants were expressed in Pichia pastoris, labeled with fluorescein 5'-isothiocyanate (FITC), and purified. Conformational changes of wild type and mutant proteins were analyzed using fluorescein fluorescence (Karlish, S. J. (1980) J. Bioenerg. Biomembr. 12, 111-136). One central finding is that the D369N/D369A mutants are strongly stabilized in E(2) compared with wild type and D369E or T212A mutants. Stabilization of E(2)(Rb) is detected by a reduced K(0.5)Rb for the Rb(+)-induced E(1) <--> E(2)(2Rb) transition. The mechanism involves a greatly reduced rate of E(2)(2Rb) --> E(1)Na with no effect on E(1) --> E(2)(2Rb). Lowering the pH from 7.5 to 5.5 strongly stabilizes wild type in E(2) but affects the D369N mutant only weakly. Thus, this 'Bohr' effect of pH on E(1) <--> E(2) is due largely to protonation of Asp(369). Two novel effects of phosphate and vanadate were observed with the D369N/D369A mutants as follows. (a) E(1) --> E(2).P is induced by phosphate without Mg(2+) ions by contrast with wild type, which requires Mg(2+). (b) Both phosphate and vanadate induce rapid E(1) --> E(2) transitions compared with slow rates for the wild type. With reference to crystal structures of Ca(2+)-ATPase and Na(+),K(+)-ATPase, negatively charged Asp(369) favors disengagement of the A domain from N and P domains (E(1)), whereas the neutral D369N/D369A mutants favor association of the A domain (TGES sequence) with P and N domains (E(2)). Changes in charge interactions of Asp(369) may play an important role in triggering E(1)P(3Na) <--> E(2)P and E(2)(2K) --> E(1)Na transitions in native Na(+),K(+)-ATPase.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	45
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-11-06
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Sodium-Potassium-Exchanging ATPase Chemistry Animals Kinetics Pichia Genetics Metabolism Protein Conformation Recombinant Proteins Swine Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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