Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.101 extracted from

  • Gardiennet, C.; Wiegand, T.; Bazin, A.; Cadalbert, R.; Kunert, B.; Lacabanne, D.; Gutsche, I.; Terradot, L.; Meier, B.; Böckmann, A.
    Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori (2016), J. Biomol. NMR, 64, 189-195 .
No PubMed abstract available
Search for more literature for 2.7.7.101

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Helicobacter pylori

Organism

Organism UniProt Comment Textmining
Helicobacter pylori P56064
-
-
Helicobacter pylori ATCC 700392 P56064
-
-

General Information

General Information Comment Organism
physiological function DnaB helicase and the C-terminal domain of the DnaG primase interact in a six to three ratio to give a complex of 387000 Da. Binding of DnaG leads to changes in the interaction interface Helicobacter pylori