3D-localization of the a -subunit in F 0 F 1 -ATP synthase by time resolved single-molecule FRET

2006 ◽  
Author(s):  
Monika G. Düser ◽  
Nawid Zarrabi ◽  
Yumin Bi ◽  
Boris Zimmermann ◽  
Stanley D. Dunn ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Single Molecule ◽  
Time Resolved ◽  
Single Molecule Fret ◽  
3D Localization ◽  
A Subunit

scholarly journals Spotlighting motors and controls of single FoF1-ATP synthase

2013 ◽  
Vol 41 (5) ◽  
pp. 1219-1226 ◽  
Author(s):  
Michael Börsch ◽  
Thomas M. Duncan
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Single Molecule ◽  
Conformational Changes ◽  
Structural Information ◽  
E Coli ◽  
Single Molecule Fret ◽  
Membrane Enzyme ◽  
Subunit Rotation ◽  
Fof1 Atp Synthase

Subunit rotation is the mechanochemical intermediate for the catalytic activity of the membrane enzyme FoF1-ATP synthase. smFRET (single-molecule FRET) studies have provided insights into the step sizes of the F1 and Fo motors, internal transient elastic energy storage and controls of the motors. To develop and interpret smFRET experiments, atomic structural information is required. The recent F1 structure of the Escherichia coli enzyme with the ϵ-subunit in an inhibitory conformation initiated a study for real-time monitoring of the conformational changes of ϵ. The present mini-review summarizes smFRET rotation experiments and previews new smFRET data on the conformational changes of the CTD (C-terminal domain) of ϵ in the E. coli enzyme.

scholarly journals Determinants of directionality and efficiency of the ATP synthase Fo motor at atomic resolution

2021 ◽  
Author(s):  
Antoni Marciniak ◽  
Pawel Chodnicki ◽  
Kazi Amirul Hossain ◽  
Joanna Slabonska ◽  
Jacek Czub
Keyword(s):  
Atp Synthase ◽  
Single Molecule ◽  
Protein Interactions ◽  
Structural Information ◽  
Mechanical Energy ◽  
Release Site ◽  
Tight Coupling ◽  
A Subunit ◽  
Energy Simulations ◽  
Rotary Motor

Fo subcomplex of ATP synthase is an 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 intra-protein 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.

Stepwise rotation of the γ-subunit of EF o F 1 -ATP synthase during ATP synthesis: a single-molecule FRET approach

2003 ◽  
Author(s):  
Michael Borsch ◽  
Manuel Diez ◽  
Boris Zimmermann ◽  
Matthias Trost ◽  
Stefan Steigmiller ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Single Molecule ◽  
Atp Synthesis ◽  
Single Molecule Fret ◽  
Γ Subunit

Structural dynamics of P-type ATPase ion pumps

2019 ◽  
Vol 47 (5) ◽  
pp. 1247-1257 ◽  
Author(s):  
Mateusz Dyla ◽  
Sara Basse Hansen ◽  
Poul Nissen ◽  
Magnus Kjaergaard
Keyword(s):  
Structural Dynamics ◽  
Single Molecule ◽  
New Technologies ◽  
Atp Hydrolysis ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Resolved ◽  
Dynamics Simulations ◽  
Types Of Information ◽  
P Type

Abstract P-type ATPases transport ions across biological membranes against concentration gradients and are essential for all cells. They use the energy from ATP hydrolysis to propel large intramolecular movements, which drive vectorial transport of ions. Tight coordination of the motions of the pump is required to couple the two spatially distant processes of ion binding and ATP hydrolysis. Here, we review our current understanding of the structural dynamics of P-type ATPases, focusing primarily on Ca2+ pumps. We integrate different types of information that report on structural dynamics, primarily time-resolved fluorescence experiments including single-molecule Förster resonance energy transfer and molecular dynamics simulations, and interpret them in the framework provided by the numerous crystal structures of sarco/endoplasmic reticulum Ca2+-ATPase. We discuss the challenges in characterizing the dynamics of membrane pumps, and the likely impact of new technologies on the field.

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