Cell
Volume 59, Issue 1, 6 October 1989, Pages 219-228
ArticleA conserved 3′→5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases
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2021, EnzymesCitation Excerpt :This activity is critical for replication fidelity during viral infection [97]; i.e., inactivating the enzyme results in much higher mutation rates (see Section 7.4). As noted above, the Exo domain contains three regions highly conserved among DNA polymerases, Exo I, Exo II, and Exo III [36]. In the cryo-EM structures (Fig. 1A and C), HSV Pol residues D368 and E370 are positioned to coordinate two metal ions required for 3′-5′ exonuclease activity, similar to that observed for RB69 Pol [46].
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