scholarly journals S09A4 Rotary mechanisms of F1-ATPase revealed by molecular simulations(Mechanism of F_1-ATPase Molecular Motor-A Cross Talk among Single Molecule, Structural Biology, and Molecular Simulation Studies-)

2007 ◽  
Vol 47 (supplement) ◽  
pp. S13
Author(s):  
Nobuyasu Koga ◽  
Shoji Takada
Keyword(s):  
Molecular Simulation ◽  
Structural Biology ◽  
Single Molecule ◽  
Cross Talk ◽  
Molecular Motor ◽  
Molecular Simulations ◽  
Simulation Studies ◽  
F1 Atpase

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 1P171 Single molecule analyses of human F1-ATPase revealed distinct rotation scheme of mitochondrial F1 motor(11.Molecular motor,Poster,The 51st Annual Meeting of the Biophysical Society of Japan)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S134
Author(s):  
Toshiharu Suzuki ◽  
Kazumi Tanaka ◽  
Chiaki Wakabayashi ◽  
Shou Furuike ◽  
Eiichiro Saita ◽  
...  
Keyword(s):  
Annual Meeting ◽  
Single Molecule ◽  
Molecular Motor ◽  
F1 Atpase ◽  
Rotation Scheme ◽  
Biophysical Society

scholarly journals F1-ATPase conformational cycle from simultaneous single-molecule FRET and rotation measurements

2016 ◽  
Vol 113 (21) ◽  
pp. E2916-E2924 ◽  
Author(s):  
Mitsuhiro Sugawa ◽  
Kei-ichi Okazaki ◽  
Masaru Kobayashi ◽  
Takashi Matsui ◽  
Gerhard Hummer ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Single Molecule ◽  
Conformational Changes ◽  
Molecular Motor ◽  
Principal Component ◽  
Structural Basis ◽  
F1 Atpase ◽  
Single Molecule Fret ◽  
Mechanochemical Coupling ◽  
Central Shaft

Despite extensive studies, the structural basis for the mechanochemical coupling in the rotary molecular motor F1-ATPase (F1) is still incomplete. We performed single-molecule FRET measurements to monitor conformational changes in the stator ring-α3β3, while simultaneously monitoring rotations of the central shaft-γ. In the ATP waiting dwell, two of three β-subunits simultaneously adopt low FRET nonclosed forms. By contrast, in the catalytic intermediate dwell, two β-subunits are simultaneously in a high FRET closed form. These differences allow us to assign crystal structures directly to both major dwell states, thus resolving a long-standing issue and establishing a firm connection between F1 structure and the rotation angle of the motor. Remarkably, a structure of F1 in an ε-inhibited state is consistent with the unique FRET signature of the ATP waiting dwell, while most crystal structures capture the structure in the catalytic dwell. Principal component analysis of the available crystal structures further clarifies the five-step conformational transitions of the αβ-dimer in the ATPase cycle, highlighting the two dominant modes: the opening/closing motions of β and the loosening/tightening motions at the αβ-interface. These results provide a new view of tripartite coupling among chemical reactions, stator conformations, and rotary angles in F1-ATPase.

scholarly journals A model of processive walking and slipping of kinesin-8 molecular motors

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ping Xie
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
External Load ◽  
Molecular Motor ◽  
Velocity Versus ◽  
Stick Slip ◽  
Load Dependence ◽  
Chemomechanical Coupling ◽  
Similarities And Differences ◽  
Stick Slip Motion

AbstractKinesin-8 molecular motor can move with superprocessivity on microtubules towards the plus end by hydrolyzing ATP molecules, depolymerizing microtubules. The available single molecule data for yeast kinesin-8 (Kip3) motor showed that its superprocessive movement is frequently interrupted by brief stick–slip motion. Here, a model is presented for the chemomechanical coupling of the kinesin-8 motor. On the basis of the model, the dynamics of Kip3 motor is studied analytically. The analytical results reproduce quantitatively the available single molecule data on velocity without including the slip and that with including the slip versus external load at saturating ATP as well as slipping velocity versus external load at saturating ADP and no ATP. Predicted results on load dependence of stepping ratio at saturating ATP and load dependence of velocity at non-saturating ATP are provided. Similarities and differences between dynamics of kinesin-8 and that of kinesin-1 are discussed.

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