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. Author manuscript; available in PMC: 2016 Oct 9.
Published in final edited form as: J Mol Biol. 2015 Aug 21;427(20):3285–3299. doi: 10.1016/j.jmb.2015.08.013

Figure 6. Pseudo-atomic model of S:L-terminase holoenzyme.

Figure 6

(A) Various views of the 3-D reconstruction in Fig. 5B colored as a transparent gray surface with docked models of one nonameric S-terminase (cyan) and two L-terminase subunits with ATPase and nuclease domains colored in red and yellow, respectively. Each L-terminase has an ATPase domain (red) and a nuclease domain (yellow) separated by a short flexible linker (black). Models were rigid-body refined into density using the “Fitmap” function in Chimera [50]. (B) Models of S:L-terminase binding to dsDNA. In model 1, dsDNA passes through the lower hole between the L-terminase domains. In model 2, the dsDNA is vertically positioned between the two L-terminase domains and abuts the S-terminase C-terminal helices. In this conformation, dsDNA could fit in the S-terminase central channel.