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Literature summary for 2.7.7.101 extracted from

  • Thirlway, J.; Turner, I.; Gibson, C.; Gardiner, L.; Brady, K.; Allen, S.; Roberts, C.; Soultanas, P.
    DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings (2004), Nucleic Acids Res., 32, 2977-2986 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus Q9X4D0
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General Information

General Information Comment Organism
physiological function DnaG interacts with the flexible linker that connects the N- and C-terminal domains of helicase DnaB. Binding of the primase to the helicase induces predominantly a 3fold symmetric morphology to the hexameric ring. Three DnaG molecules interact with the hexameric ring helicase, with a small number of complexes with two and even one DnaG molecule bound to DnaB also detected Geobacillus stearothermophilus