Key result
Opening the myosin Arg-Glu salt bridge fails to promote back-door phosphate egress in computational models.
Why the study?
The process and effects of opening the Arg-Glu salt bridge in myosin after ATP hydrolysis were not fully understood.
Computational modeling suggests that opening the Arg-Glu salt bridge in myosin is facilitated after ATP hydrolysis but does not promote inorganic phosphate egress via the back-door mechanism.
Answers are grounded in this paper and cite their sources.
Salt bridge opening facilitated after hydrolysis without promoting egress; leaves open its role in myosin product release pending validation.
Opening the Arg-Glu salt bridge in myosin, which presumably succeeds the myosin-catalyzed hydrolysis of adenosine triphosphate, was modeled computationally on the basis of the structures corresponding to the enzyme-substrate and enzyme-product complexes found in the quantum mechanics-molecular mechanics simulations. According to the calculations of the potential of mean force, opening the bridge is considerably facilitated upon termination of the chemical reaction, but does not promote egress of inorganic phosphate by the back-door mechanism.
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Kaliman et al. (2009) studied this question. Opening the Arg-Glu salt bridge in myosin was evaluated on Potential of mean force and egress of inorganic phosphate. Computational modeling indicates that opening the Arg-Glu salt bridge in myosin is facilitated after ATP hydrolysis but does not promote egress of inorganic phosphate by the back-door mechanism.
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