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Figure 2 | Cell & Bioscience

Figure 2

From: Nanobiomotors of archaeal DNA repair machineries: current research status and application potential

Figure 2

(A) Rotation model by SF2 helicase (adapted from Buttner et al. [34]). This type of nanobiomotor works as monomers and DNA unwinding occurs in two steps: (1) ATP binding leads to a structural change of the enzyme which pushes the two helicase domains closer. After ATP hydrolysis and ADP release, the protein conformation resets, resulting in a movement of the protein along DNA. (B). Rotatory inchworm model by Ftsk (adapted from Massey et al. [46]). Each subunit moves along the DNA molecule in an inchworm manner as illustrated in 2A. Conformation change of the two DNA-binding sites in Subunit 1 (marked with stars) will lead to the interaction between DNA and the adjacent subunit (Subunit 2) due to the helical nature of DNA. Then, Subunit 2 completes its translocation upon ATP hydrolysis and ADP release, facilitating the interaction between Subunit 3 and the DNA target, and the cycle continues. Together, all subunits work sequentially with the rotation of the binding sites around the hexamer and the system proceeds like a rotatory inchworm. The arrow indicates the direction of DNA translocation.

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