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. Author manuscript; available in PMC: 2008 Mar 7.
Published in final edited form as: Mol Cell. 2007 Dec 28;28(6):1058–1070. doi: 10.1016/j.molcel.2007.10.025

Figure 7. RecA and UmuD2 may enclose the open active site of DinB.

Figure 7

A–B. In silico modeling of a ternary complex of the proteins. The surface representation of DinB is shown in blue, UmuD2 in yellow, and RecA in orange. The DNA is relatively enclosed in the complex. C. Statistical covariance of DinB/pol κ residues across evolution. Residues that display statistical covariance with the UmuD2 binding interface on E. coli DinB define an interface in a similar position on pol κ (shown in red), suggesting a possible rationale for the maintenance of this interface as a site of regulatory protein-protein interactions.