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

BRENDA support

Literature summary for 2.7.7.101 extracted from

  • Bergsch, J.; Allain, F.H.; Lipps, G.
    Recent advances in understanding bacterial and archaeoeukaryotic primases (2019), Curr. Opin. Struct. Biol., 59, 159-167 .
    View publication on PubMed
Search for more literature for 2.7.7.101

Activating Compound

Activating Compound Comment Organism Structure
DnaB DnaG is activated about 5000fold when bound to DnaB Geobacillus stearothermophilus
DnaB DnaG is activated about 5000fold when bound to DnaB Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ssDNA + n NTP Geobacillus stearothermophilus
-
 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
ssDNA + n NTP Escherichia coli
-
 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABS5
-
-
Geobacillus stearothermophilus Q9X4D0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ssDNA + n NTP
-
 Geobacillus stearothermophilus ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?
ssDNA + n NTP
-
 Escherichia coli ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?

Subunits

Subunits Comment Organism
More DnaG is organized in three domains, the N-terminal zinc-binding domain (ZBD), the central RNA polymerase domain (RPD) and the C-terminal helicase-binding domain (HBD). The role of the ZBD is to recognize the priming site, which is 5'-C(A/T)G. The RPD carries the active site with three catalytic acidic residues that are exposed at a cleft in the center of the protein. This part of the proteins has structural similarity with the toprim fold, a region of about 100 amino acids found in topoisomerases. The HBD anchors the primase at the hexameric ring of the helicase. The latter interaction is particularly important as DnaG is activated about 5000fold when bound to DnaB. Within the replisome, two DnaG molecules cooperate, one molecule binding the template at the trinucleotide priming site and the other catalyzing primer synthesis Geobacillus stearothermophilus
More DnaG is organized in three domains, the N-terminal zinc-binding domain (ZBD), the central RNA polymerase domain (RPD) and the C-terminal helicase-binding domain (HBD). The role of the ZBD is to recognize the priming site, which is 5'-C(A/T)G. The RPD carries the active site with three catalytic acidic residues that are exposed at a cleft in the center of the protein. This part of the proteins has structural similarity with the toprim fold, a region of about 100 amino acids found in topoisomerases. The HBD anchors the primase at the hexameric ring of the helicase. The latter interaction is particularly important as DnaG is activated about 5000fold when bound to DnaB. Within the replisome, two DnaG molecules cooperate, one molecule binding the template at the trinucleotide priming site and the other catalyzing primer synthesis Escherichia coli

Synonyms

Synonyms Comment Organism
DnaG
-
 Geobacillus stearothermophilus
DnaG
-
 Escherichia coli
primase DnaG
-
 Geobacillus stearothermophilus
primase DnaG
-
 Escherichia coli

General Information

General Information Comment Organism
additional information structure of bacterial primase DnaG in complex with the bacterial replicative helicase DnaB, structure comparisons, overview Geobacillus stearothermophilus
additional information structure of bacterial primase DnaG in complex with the bacterial replicative helicase DnaB, structure comparisons, overview Escherichia coli