The Phylogenetic Signature Underlying ATP Synthase c-Ring Compliance

Biophysical Journal
Alessandro PandiniShahid Khan

Abstract

The proton-driven ATP synthase (FOF1) is comprised of two rotary, stepping motors (FO and F1) coupled by an elastic power transmission. The elastic compliance resides in the rotor module that includes the membrane-embedded FO c-ring. Proton transport by FO is firmly coupled to the rotation of the c-ring relative to other FO subunits (ab2). It drives ATP synthesis. We used a computational method to investigate the contribution of the c-ring to the total elastic compliance. We performed principal component analysis of conformational ensembles built using distance constraints from the bovine mitochondrial c-ring x-ray structure. Angular rotary twist, the dominant ring motion, was estimated to show that the c-ring accounted in part for the measured compliance. Ring rotation was entrained to rotation of the external helix within each hairpin-shaped c-subunit in the ring. Ensembles of monomer and dimers extracted from complete c-rings showed that the coupling between collective ring and the individual subunit motions was independent of the size of the c-ring, which varies between organisms. Molecular determinants were identified by covariance analysis of residue coevolution and structural-alphabet-based local dynamics correlations. T...Continue Reading

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Citations

Jun 28, 2016·Structure·Alessandro PandiniShahid Khan
Dec 19, 2017·Evidence-based Complementary and Alternative Medicine : ECAM·Qing GaoXijuan Jiang
Jun 1, 2019·PLoS Computational Biology·Alessandro PandiniShahid Khan
Nov 7, 2017·PLoS Computational Biology·Shaima HashemArianna Fornili
Sep 7, 2020·Biophysical Journal·Paige WheatleyShahid Khan

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Methods Mentioned

BETA
nuclear magnetic resonance
NMR
PCA
electron cryo-microscopy

Software Mentioned

GROMACS
tCONCOORD
PYMOL
R
HMMER
ROCR
GNM
PSICOV
PCA
MD

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