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. Author manuscript; available in PMC: 2012 Oct 1.
Published in final edited form as: Curr Opin Chem Biol. 2011 Sep 9;15(5):580–586. doi: 10.1016/j.cbpa.2011.07.024

Figure 2.

Figure 2

Three modes of interactions between gp4 and gp5/trx during leading strand synthesis. (a) Gp5/trx is loaded onto the hexameric gp4 through an interaction of the acidic C-terminal tail of gp4 with a basic patch at the front side (Fbp) of gp5. (b) A high affinity complex between the two proteins coordinates their activities during DNA synthesis. (c) Gp5/trx temporarily dissociated from gp4 or present in solution is retained with gp4 through an interaction between two basic loops in the trx binding domain (TBDbp) of gp5 and the acidic C-terminal tail of gp4.