Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2021 Feb 3;49(4):2161–2178. doi: 10.1093/nar/gkab042

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2021. 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/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 5. — ATPase-driven DNA translocation by SauUSI. (A) The primary domain architecture of the SF2-helicase like ATPase along with the canonical motifs marked in specific colors. The canonical motifs of the SF2-helicase like ATPase of SauUSI are compared to that of LlaBIII (Type ISP REase), HsdR (Type I REase) and EcoP15I (Type III REase). (B) Structure of the ATPase domain with the two RecA folds colored distinctly. The catalytically important Walker A and Walker B residues, along with a sulfate ion (shown as a sphere) bound at the ATP binding site are shown. Also, illustrated are the other canonical motifs in the same color code as in panel A. (C) The DNA used for the triplex displacement assay has an enzyme binding cassette located 604 bp away from the triplex binding site. A representative PAGE gel of the triplex displacement assay carried out over a time period of 1–10 min. (D) Translocase activity of SauUSI^H119A monitored by the percentage of triplex displaced as a function of time (n = 3).