Abstract
DNA primase is a DNA-dependent RNA polymerase that synthesizes short oligonucleotide primers required for processive DNA replication. Like many enzymes involved in DNA replication and repair, human DNA primase contains a redox-active, high potential [4Fe4S] cluster whose associated redox state serves as an on/off “switch” for DNA binding. The structural basis for this “switch,” however, is poorly understood, given the 25 Å distance between the [4Fe4S] cluster and DNA binding region. Examination of available crystallographic data suggests the [4Fe4S] cluster may undergo a change in structure upon substrate binding, but this information alone is not sufficient to form conclusions about allostery.
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