Mutants of DNA polymerase I from Thermus aquaticus (Taq) with higher fidelity compared to the wild type enzyme were identified in an earlier study by Summerer et al. (Angew Chem Int Ed 44:4712-4715, 2005). Here, one of these mutants, PLQ (consensus residues 879-881), was analysed using molecular dynamics simulations. This was done by calculating the structures of the ternary complex comprising the enzyme, the DNA primer and template as well as the incoming nucleotide before the chemical reaction for the Watson-Crick and different mismatched base pairings. The results show that the high fidelity of the mutant can be explained partly by different specific interactions between the amino acids of the enzyme and the DNA primer end as well as, in some mismatches, a displacement of the primer relative to the incoming deoxyribonucleoside triphosphate and the catalytic magnesium ion. This displacement is facilitated by reduced steric interactions between the enzyme and the DNA.