Skip to main content
. Author manuscript; available in PMC: 2012 Dec 1.
Published in final edited form as: Nat Struct Mol Biol. 2012 May 6;19(6):628–632. doi: 10.1038/nsmb.2295

Figure 3.

Figure 3

Close-up views of the active site regions of human Polη ternary complexes bound to (a) PtGpG DNA, and (b) cis-syn T-T dimer DNA8 (PDB 3MR3) The palm, fingers and PAD domains are shown in cyan, yellow and green, respectively. The DNA is colored grey, incoming nucleotide is in red and the putative Mg2+ ions are dark blue in both the structures. The residues are colored to match the color of their respective domains. Highlighted and labeled are the catalytic residues (Asp13, Asp115 and Glu116), and residues that interact with the triphosphate moiety of incoming nucleotide (Tyr52, Arg55). Arg61 has one conformation in the PtGpG ternary complex where it interacts with the incoming dCTP, in contrast it adopts multiple conformations in the cis-syn T-T dimer ternary complex.