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Determinants of Directionality and Efficiency of the ATP Synthase Fo Motor at Atomic Resolution

Abstract

Fo subcomplex of ATP synthase is a membrane-embedded rotary motor that converts proton motive force into mechanical energy. Despite a rapid increase in the number of high-resolution structures, the mechanism of tight coupling between proton transport and motion of the rotary c-ring remains elusive. Here, using extensive all-atom free energy simulations, we show how the motor’s directionality naturally arises from the interplay between intraprotein interactions and energetics of protonation of the c-ring. Notably, our calculations reveal that the strictly conserved arginine in the a-subunit (R176) serves as a jack-of-all-trades: it dictates the direction of rotation, controls the protonation state of the proton-release site, and separates the two proton-access half-channels. Therefore, arginine is necessary to avoid slippage between the proton flux and the mechanical output and guarantees highly efficient energy conversion. We also provide mechanistic explanations for the reported defective mutations of R176, reconciling the structural information on the Fo motor with previous functional and single-molecule data.

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Details

Category:
Articles
Type:
artykuły w czasopismach
Published in:
Journal of Physical Chemistry Letters no. 13, pages 387 - 392,
ISSN: 1948-7185
Language:
English
Publication year:
2022
Bibliographic description:
Marciniak A., Chodnicki P., Hossain K., Słabońska J., Czub J.: Determinants of Directionality and Efficiency of the ATP Synthase Fo Motor at Atomic Resolution// Journal of Physical Chemistry Letters -Vol. 13,iss. 1 (2022), s.387-392
DOI:
Digital Object Identifier (open in new tab) 10.1021/acs.jpclett.1c03358
Sources of funding:
  • Free publication
Verified by:
Gdańsk University of Technology

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