Literature summary for 2.7.7.101 extracted from

Bailey, S.; Eliason, W.; Steitz, T.
Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase (2007), Science, 318, 459-463 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of hexameric helicase DnaB and its complex with the helicase binding domain of DnaG. Within the hexamer the two domains of DnaB pack with different symmetries to form a distinct two-layered ring structure. Each of three bound DnaG helicase binding domains stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and guide the DNA to a DnaG active site	Geobacillus stearothermophilus

Crystallization (Comment)

Organism

structures of hexameric helicase DnaB and its complex with the helicase binding domain of DnaG. Within the hexamer the two domains of DnaB pack with different symmetries to form a distinct two-layered ring structure. Each of three bound DnaG helicase binding domains stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and guide the DNA to a DnaG active site

Geobacillus stearothermophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	Q9X4D0	-	-

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Release 2023.1 (January 2023)