Molecular Mechanism of ATP Hydrolysis in F1-ATPase Revealed by Molecular Simulations and Single-Molecule Observations

2012 ◽  
Vol 134 (20) ◽  
pp. 8447-8454 ◽  
Author(s):  
Shigehiko Hayashi ◽  
Hiroshi Ueno ◽  
Abdul Rajjak Shaikh ◽  
Myco Umemura ◽  
Motoshi Kamiya ◽  
...  
Keyword(s):  
Molecular Mechanism ◽  
Single Molecule ◽  
Atp Hydrolysis ◽  
Molecular Simulations ◽  
F1 Atpase

scholarly journals Simple mechanism whereby the F1-ATPase motor rotates with near-perfect chemomechanical energy conversion

2015 ◽  
Vol 112 (31) ◽  
pp. 9626-9631 ◽  
Author(s):  
Ei-ichiro Saita ◽  
Toshiharu Suzuki ◽  
Kazuhiko Kinosita ◽  
Masasuke Yoshida
Keyword(s):  
Physical Model ◽  
Single Molecule ◽  
Atp Hydrolysis ◽  
Rotation Angle ◽  
Mechanical Work ◽  
F1 Atpase ◽  
The Third ◽  
Γ Subunit ◽  
Simple Physical Model ◽  
Central Shaft

F1-ATPase is a motor enzyme in which a central shaft γ subunit rotates 120° per ATP in the cylinder made of α3β3 subunits. During rotation, the chemical energy of ATP hydrolysis (ΔGATP) is converted almost entirely into mechanical work by an elusive mechanism. We measured the force for rotation (torque) under various ΔGATP conditions as a function of rotation angles of the γ subunit with quasi-static, single-molecule manipulation and estimated mechanical work (torque × traveled angle) from the area of the function. The torque functions show three sawtooth-like repeats of a steep jump and linear descent in one catalytic turnover, indicating a simple physical model in which the motor is driven by three springs aligned along a 120° rotation angle. Although the second spring is unaffected by ΔGATP, activation of the first spring (timing of the torque jump) delays at low [ATP] (or high [ADP]) and activation of the third spring delays at high [Pi]. These shifts decrease the size and area of the sawtooth (magnitude of the work). Thus, F1-ATPase responds to the change of ΔGATP by shifting the torque jump timing and uses ΔGATP for the mechanical work with near-perfect efficiency.

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.

scholarly journals Single-molecule approach to compare the rotation of F1-ATPase with the archaeal A1-ATPase

2014 ◽  
Vol 1837 ◽  
pp. e21
Author(s):  
Hendrik Sielaff ◽  
Dhirendra Singh ◽  
Lavanya Sundaraman ◽  
Ardina Grüber ◽  
Gerhard Grüber
Keyword(s):  
Single Molecule ◽  
F1 Atpase ◽  
A1 Atpase

scholarly journals Single–motor mechanics and models of the myosin motor

2000 ◽  
Vol 355 (1396) ◽  
pp. 441-447 ◽  
Author(s):  
T. Yanagida ◽  
S. Esaki ◽  
A. Hikikoshi Iwane ◽  
Y. Inoue ◽  
A. Ishijima ◽  
...  
Keyword(s):  
Single Molecule ◽  
Atp Hydrolysis ◽  
Accurate Determination ◽  
Step Size ◽  
Single Molecule Level ◽  
Detection Techniques ◽  
Myosin Motor ◽  
Mechanochemical Coupling ◽  
Chemical Events

Recent progress in single–molecule detection techniques is remarkable. These techniques have allowed the accurate determination of myosin–head–induced displacements and how mechanical cycles are coupled to ATP hydrolysis, by measuring individual mechanical events and chemical events of actomyosin directly at the single–molecule level. Here we review our recent work in which we have made detailed measurements of myosin step size and mechanochemical coupling, and propose a model of the myosin motor.

Molecular mechanism of the selectivity between BAFF/APRIL and their receptors by molecular simulations

2017 ◽  
Vol 43 (8) ◽  
pp. 590-598 ◽  
Author(s):  
Xuegang Fu ◽  
Zhuo Mao ◽  
Siming Li ◽  
Yunyun Guan ◽  
Xiaodong Jian ◽  
...  
Keyword(s):  
Molecular Mechanism ◽  
Molecular Simulations

scholarly journals 2P194 Single molecule observation of ATP hydrolysis of Myosin V

2005 ◽  
Vol 45 (supplement) ◽  
pp. S168
Author(s):  
T. Komori ◽  
S. Nishikawa ◽  
T. Ariga ◽  
A.H. Iwane ◽  
H. Yamakawa ◽  
...  
Keyword(s):  
Single Molecule ◽  
Atp Hydrolysis ◽  
Myosin V ◽  
Hydrolysis Of
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