Structural basis for power stroke vs. Brownian ratchet mechanisms of motor proteins.
basic_science · Level V
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- Record sourced from PubMed, PMID 31506355.
- Also identified by DOI 10.1073/pnas.1818589116 and PMC identifier 6778177.
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Abstract
Two mechanisms have been proposed for the function of motor proteins: The power stroke and the Brownian ratchet. The former refers to generation of a large downhill free energy gradient over which the motor protein moves nearly irreversibly in making a step, whereas the latter refers to biasing or rectifying the diffusive motion of the motor. Both mechanisms require input of free energy, which generally involves the processing of an ATP (adenosine 5'-triphosphate) molecule. Recent advances in experiments that reveal the details of the stepping motion of motor proteins, together with computer simulations of atomistic structures, have provided greater insights into the mechanisms. Here, we compare the various models of the power stroke and the Brownian ratchet that have been proposed. The 2 mechanisms are not mutually exclusive, and various motor proteins employ them to different extents to perform their biological function. As examples, we discuss linear motor proteins Kinesin-1 and myosin-V, and the rotary motor F<sub>1</sub>-ATPase, all of which involve a power stroke as the essential element of their stepping mechanism.
Medical subject headings
- Adenosine Triphosphate
- Kinesins
- Myosin Type V
- Myosins
- Proton-Translocating ATPases