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Control of a biomolecular motor-powered nanodevice with an engineered chemical switch


The biophysical and biochemical properties of motor proteins have been well-studied, but these motors also show promise as mechanical components in hybrid nano-engineered systems1,2,3,4. The cytoplasmic F1 fragment of the adenosine triphosphate synthase (F1-ATPase) can function as an ATP-fuelled rotary motor4,5,6,7 and has been integrated into self-assembled nanomechanical systems as a mechanical actuator4,8. Here we present the rational design, construction and analysis of a mutant F1-ATPase motor containing a metal-binding site that functions as a zinc-dependent, reversible on/off switch. Repeated cycles of zinc addition and removal by chelation result in inhibition and restoration, respectively, of both ATP hydrolysis and motor rotation of the mutant, but not of the wild-type F1 fragment. These results demonstrate the ability to engineer chemical regulation into a biomolecular motor and represent a critical step towards controlling integrated nanomechanical devices at the single-molecule level.

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Figure 1: Molecular model of the computationally designed Zn2+ binding site in the bovine F1-ATPase.
Figure 2: Steady-state kinetics of ATP hydrolysis in the wild-type and mutant TF1 enzymes.
Figure 3: Measurements of single-molecule rotation and control.


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We thank C. Xu for help in the protein modelling of the TF1 structure. This research was supported in part by grants from NASA (NAG5-8775), DARPA (N00014-99-1-0436) and NSF (ECS-0084732). Sandia is a multiprogram laboratory operated by Sandia Corporation, a Lockheed Martin Company, for the US Department of Energy under contract DE-AC04-94AL85000.

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Correspondence to Carlo D. Montemagno.

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Liu, H., Schmidt, J., Bachand, G. et al. Control of a biomolecular motor-powered nanodevice with an engineered chemical switch. Nature Mater 1, 173–177 (2002).

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