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. Author manuscript; available in PMC: 2013 Nov 13.
Published in final edited form as: Biochemistry. 2012 Oct 30;51(45):9234–9244. doi: 10.1021/bi301043k

Figure 6.

Figure 6

Dpo4 binds N-MC-dAMP in a manner that closely resembles unmodified dATP. (a) The Dpo4•North structure is shown superimposed with wild-type Dpo4 in complex with dATP (PDB code 2AGQ, light red carbons) and a steric-gate mutant form of Dpo4 (Y12A) bound to ADP (PDB code 3PR5, yellow carbons). (b) The active site base pairing modes in panel a are shown rotated approximately 90° to illustrate the orientation relative to the primer terminus. The side-chains at position 12 and 51 of the Dpo4 proteins are shown.