Abrahams

Banghart

Beharry

Bonardi

Boyer

Cingolani

DeLeon-Rangel

Duncan

Greene

Hanwell

Hoersch

Itoh

Junge

Kaplan

Kinosita

Kumita

Mayer

Milgrom

Morales-Rios

Noji

Numano

Okuno

Ritterson

Rondelez

Sabbert

Schafer

Schierling

Schneider

Sielaff

Szymański

Umeki

Volgraf

Walker

Zhang

PeerJ

English

The F1sub-complex of ATP synthase is a biological nanomotor that converts the free energy of ATP hydrolysis into mechanical work with an astonishing efficiency of up to 100% (Kinosita et al., 2000). To probe the principal mechanics of the machine, I re-engineered the active site ofE.coliF1ATPase with a structure-based protein design approach: by incorporation of a site-specific, photoswitchable crosslinker, whose end-to-end distance can be modulated by illumination with light of two different wavelengths, a dynamic constraint was imposed on the inter-atomic distances of the α and β subunits. Crosslinking reduced the ATP hydrolysis activity of four designs tested in vitro and in one case created a synthetic ATPase whose activity can be reversibly modulated by subsequent illumination with near UV and blue light. The work is a first step into the direction of the long-term goal to design nanoscaled machines based on biological parts that can be precisely controlled by light.</jats:p

Daniel Hoersch

Crossref

Engineering a light-controlled F<sub>1</sub>ATPase using structure-based protein design

Supplemental Information 5: Data for Fig. 2D.

Supplemental Information 5: Data for Fig. 2D.

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