scholarly journals ATP hydrolysis-driven structural changes in the gamma-subunit of Escherichia coli ATPase monitored by fluorescence from probes bound at introduced cysteine residues.

1994 ◽  
Vol 269 (18) ◽  
pp. 13465-13471
Author(s):  
P. Turina ◽  
R.A. Capaldi
Keyword(s):  
Escherichia Coli ◽  
Structural Changes ◽  
Atp Hydrolysis ◽  
Cysteine Residues ◽  
Gamma Subunit

scholarly journals A Model of the Quaternary Structure of the Escherichia coli F1 ATPase from X-Ray Solution Scattering and Evidence for Structural Changes in the Delta Subunit during ATP Hydrolysis

1998 ◽  
Vol 75 (5) ◽  
pp. 2212-2219 ◽  
Author(s):  
Dmitri I. Svergun ◽  
Ingo Aldag ◽  
Tanja Sieck ◽  
Karlheinz Altendorf ◽  
Michel H.J. Koch ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Changes ◽  
Quaternary Structure ◽  
Atp Hydrolysis ◽  
X Ray ◽  
F1 Atpase ◽  
Delta Subunit

Structural changes in 16S RNA from Escherichia coli upon unfolding by urea

Biopolymers ◽  
1993 ◽  
Vol 33 (11) ◽  
pp. 1747-1755 ◽  
Author(s):  
A. A. Timchenko ◽  
J. Langowski ◽  
I. N. Serdyuk
Keyword(s):  
Escherichia Coli ◽  
Structural Changes ◽  
16S Rna

scholarly journals Unraveling a Force-Generating Allosteric Pathway of Actomyosin Communication Associated with ADP and Pi Release

2020 ◽  
Vol 22 (1) ◽  
pp. 104
Author(s):  
Peter Franz ◽  
Wiebke Ewert ◽  
Matthias Preller ◽  
Georgios Tsiavaliaris
Keyword(s):  
Structural Changes ◽  
Atp Hydrolysis ◽  
Power Stroke ◽  
Duty Ratio ◽  
Prolonged Duration ◽  
Adp Release ◽  
Strong Transition ◽  
Cleft Closure ◽  
Kinetic Investigations ◽  
Allosteric Pathway

The actomyosin system generates mechanical work with the execution of the power stroke, an ATP-driven, two-step rotational swing of the myosin-neck that occurs post ATP hydrolysis during the transition from weakly to strongly actin-bound myosin states concomitant with Pi release and prior to ADP dissociation. The activating role of actin on product release and force generation is well documented; however, the communication paths associated with weak-to-strong transitions are poorly characterized. With the aid of mutant analyses based on kinetic investigations and simulations, we identified the W-helix as an important hub coupling the structural changes of switch elements during ATP hydrolysis to temporally controlled interactions with actin that are passed to the central transducer and converter. Disturbing the W-helix/transducer pathway increased actin-activated ATP turnover and reduced motor performance as a consequence of prolonged duration of the strongly actin-attached states. Actin-triggered Pi release was accelerated, while ADP release considerably decelerated, both limiting maximum ATPase, thus transforming myosin-2 into a high-duty-ratio motor. This kinetic signature of the mutant allowed us to define the fractional occupancies of intermediate states during the ATPase cycle providing evidence that myosin populates a cleft-closure state of strong actin interaction during the weak-to-strong transition with bound hydrolysis products before accomplishing the power stroke.

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