Here we present the 8 Å resolution cryo-electron microscopy structures of DNA-bound and DNA-free states of the PolIII-clamp-exonuclease-τ c complex. Due to the dynamic nature of the four-protein complex it has long been refractory to structural characterization. For its activity it relies on the DNA sliding clamp β, the proofreading exonuclease ε and the C-terminal domain of the clamp loader subunit τ. The replicative DNA polymerase PolIIIα from Escherichia coli is a uniquely fast and processive enzyme.
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