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DNA polymerase III beta subunit, C-terminal domain
A dimer of the beta subunit of DNA polymerase beta forms a ring which encircles duplex DNA. Each monomer contains three domains of identical topology and DNA clamp fold. [1]. 1349852. Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Kong XP, Onrust R, O'Donnell M, Kuriyan J;. Cell 1992;69:425-437. (from Pfam)
DNA polymerase III beta subunit, N-terminal domain
DNA polymerase III subunit beta
DNA polymerase III subunit beta act as a processivity factor, or a sliding clamp, for a wide variety of proteins that act on DNA including DNA polymerases, DNA ligase, endonucleases and glycosylases similar to Deinococcus radiodurans beta-clamp which has an evenly distributed electrostatic surface charge on the DNA interacting side that may facilitate efficient movement on encircled DNA and help ensure efficient DNA metabolism upon exposure to high doses of ionizing irradiation or desiccation
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