Two-component molecular motor driven by a GTPase cycle - Nature Physics

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Two-component molecular motor driven by a GTPase cycle - Nature Physics
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Researchers discover an alternative to ATP for string-shaped motors in cells tudresden_de NaturePhysics

, our work shows that EEA1—a prominent example of a long coiled-coil tethering molecule—is poised at a critical point close to bistable flexibility states. The switch between these states is mediated by a series of chemical steps that induce large-scale movements on the order of ~100 nm. The mechanism described here could be shared by several other protein tethers.

The model we identified to harness mechanical work from this cyclically acting polymer motor is reminiscent of a classical Stirling engine. Although classical engines use gas as the working substrate and exploit temperature gradients to generate mechanical work via expansion/compression of the gas, the two-component polymer motor that we describe here uses the polymer itself as a working substrate with flexibility changes resulting in force generation.

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