It enters the exonuclease active site, where the mismatched bond is hydrolytically cleaved. The palm domain of the enzyme closes around the reacting groups, creating an environment that excludes water.
Dynamic Interaction Between Protein and DNA Substrate During Nucleotide Addition
The structural rearrangement effectively "locks" the correct base in place before the bond is finalized. Induced Fit And Structural Rearrangement The actual chemistry involves a nucleophilic attack by the 3' hydroxyl group of the growing chain.
The Template-And-Nutrient Principle The core principle governing how DNA polymerase adds nucleotides is strict complementarity. The process is a dynamic interaction between the protein, the DNA substrate, and the incoming nucleoside triphosphate.
Dynamic Interaction Between Protein and DNA Substrate During Nucleotide Addition
The result is the formation of a phosphodiester bond that links the new nucleotide to the chain. This induced fit aligns the reactive chemistry perfectly and excludes incorrect nucleotides that lack the proper geometry.
More About How does dna polymerase add nucleotides
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