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Full-Text Articles in Biochemistry
Domain Compliance And Elastic Power Transmission In Rotary F(O)F(1)-Atpase., Hendrik Sielaff, Henning Rennekamp, André Wächter, Hao Xie, Florian Hilbers, Katrin Feldbauer, Stanley D Dunn, Siegfried Engelbrecht, Wolfgang Junge
Domain Compliance And Elastic Power Transmission In Rotary F(O)F(1)-Atpase., Hendrik Sielaff, Henning Rennekamp, André Wächter, Hao Xie, Florian Hilbers, Katrin Feldbauer, Stanley D Dunn, Siegfried Engelbrecht, Wolfgang Junge
Biochemistry Publications
The 2 nanomotors of rotary ATP synthase, ionmotive F(O) and chemically active F(1), are mechanically coupled by a central rotor and an eccentric bearing. Both motors rotate, with 3 steps in F(1) and 10-15 in F(O). Simulation by statistical mechanics has revealed that an elastic power transmission is required for a high rate of coupled turnover. Here, we investigate the distribution in the F(O)F(1) structure of compliant and stiff domains. The compliance of certain domains was restricted by engineered disulfide bridges between rotor and stator, and the torsional stiffness (kappa) of unrestricted domains was determined by analyzing their thermal rotary …
The Stator Complex Of The A1a0-Atp Synthase--Structural Characterization Of The E And H Subunits., Erik Kish-Trier, Lee-Ann K Briere, Stanley D Dunn, Stephan Wilkens
The Stator Complex Of The A1a0-Atp Synthase--Structural Characterization Of The E And H Subunits., Erik Kish-Trier, Lee-Ann K Briere, Stanley D Dunn, Stephan Wilkens
Biochemistry Publications
Archaeal ATP synthase (A-ATPase) is the functional homolog to the ATP synthase found in bacteria, mitochondria and chloroplasts, but the enzyme is structurally more related to the proton-pumping vacuolar ATPase found in the endomembrane system of eukaryotes. We have cloned, overexpressed and characterized the stator-forming subunits E and H of the A-ATPase from the thermoacidophilic Archaeon, Thermoplasma acidophilum. Size exclusion chromatography, CD, matrix-assisted laser desorption ionization time-of-flight mass spectrometry and NMR spectroscopic experiments indicate that both polypeptides have a tendency to form dimers and higher oligomers in solution. However, when expressed together or reconstituted, the two individual polypeptides interact with …