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. 2016 Jan 24;44(6):2949–2961. doi: 10.1093/nar/gkw033

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© The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 7. — Mechanism of BsPif1-catalyzed DNA unwinding. (A) ssDNA is in the binding site, 2B domain is in the upper position. (B) 2B domain rotates upon ssDNA. A tunnel is formed by 2B and 1B domains, where only ssDNA can pass through. (C) Upon nucleotide hydrolysis or exchange, the two RecA domains 1A and 2A act as molecular motor to move ssDNA by one base. The 2B domain acts as a wedge, blocking the incoming duplex. The translocation force may be sufficient to open dsDNA on the 2B wedge. (D) The 2B domain rotates back for a new cycle.