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On the Functional Role of the ε Subunit of the Molecular Motor F -Adenosine Triphosphatase in Lipid Membranes of Cells

On the Functional Role of the ε Subunit of the Molecular Motor F -Adenosine Triphosphatase in... Abstract The effect of the e subunit of the molecular motor F-adenosine triphosphatase, which is built into the lipid membrane of a cell, on the dynamics of the rotor (γ subunit), with which this subunit is bound, has been qualitatively considered. It is shown that its structural and conformational features arising during the hydrolysis of “fuel” adenosine triphosphate (ATP) molecules can be explained by the change in the potential within which the rotor is located. As the numerical calculations showed, at a low ATP concentration, the hydrolysis is accompanied by an unstable rotation of the γ subunit and the related proton current. A model is proposed to describe the interaction between the ε subunit and the lipid order fluctuations caused by the membrane transition to the gel state. It is demonstrated that the rotor rotations become inhomogeneous when this interaction is enhanced with a decrease in the cell temperature. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Crystallography Reports Springer Journals

On the Functional Role of the ε Subunit of the Molecular Motor F -Adenosine Triphosphatase in Lipid Membranes of Cells

Pikin, S. A.; Loginov, E. B.
Crystallography Reports , Volume 55 (6): 6 – Nov 1, 2010
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References (14)

Publisher
Springer Journals
Copyright
2010 Pleiades Publishing, Ltd.
ISSN
1063-7745
eISSN
1562-689X
DOI
10.1134/S1063774510060052
Publisher site
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Abstract

Abstract The effect of the e subunit of the molecular motor F-adenosine triphosphatase, which is built into the lipid membrane of a cell, on the dynamics of the rotor (γ subunit), with which this subunit is bound, has been qualitatively considered. It is shown that its structural and conformational features arising during the hydrolysis of “fuel” adenosine triphosphate (ATP) molecules can be explained by the change in the potential within which the rotor is located. As the numerical calculations showed, at a low ATP concentration, the hydrolysis is accompanied by an unstable rotation of the γ subunit and the related proton current. A model is proposed to describe the interaction between the ε subunit and the lipid order fluctuations caused by the membrane transition to the gel state. It is demonstrated that the rotor rotations become inhomogeneous when this interaction is enhanced with a decrease in the cell temperature.

Journal

Crystallography Reports – Springer Journals

Published: Nov 1, 2010

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