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Literature summary for 2.7.7.101 extracted from

  • Catazaro, J.; Periago, J.; Shortridge, M.D.; Worley, B.; Kirchner, A.; Powers, R.; Griep, M.A.
    Identification of a ligand-binding site on the Staphylococcus aureus DnaG primase C-terminal domain (2017), Biochemistry, 56, 932-943 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.101

Activating Compound

Activating Compound Comment Organism Structure
DnaC helicase DnaG primase is stimulated by the homohexameric DnaB helicase, termed DnaC helicase in Staphylococcus aureus Staphylococcus aureus

Application

Application Comment Organism
drug development the DnaG-DnaB interaction is an attractive antibiotic target because it is conserved in bacteria, essential for DNA replication, and is distinctly different from that of viruses, archaea, and eukaryotes Staphylococcus aureus

Inhibitors

Inhibitors Comment Organism Structure
additional information high-throughput NMR ligand affinity screen of the Staphylococcus aureus primase CTD. Acycloguanosine, adenosine, and myricetin bind poorly to the enzyme's C-terminal domain. Measurement of protein chemical shift perturbations (CSPs), the KD's are greater than 4 mM Staphylococcus aureus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus O05338
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ssDNA + n NTP
-
 Staphylococcus aureus ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
 ?

Subunits

Subunits Comment Organism
More DnaG primase is composed of three functional domains: the N-terminal zinc-binding domain (ZBD) responsible for DNA binding specificity, the RNA polymerase domain (RPD) responsible for enzymatic activity, and the C-terminal domain (CTD) responsible for the interaction with the DnaB helicase. Structure determination and anaysis of the C-terminal domain (CTD), solution structure and dynamics of the DnaG primase CTD, conformations and flexibility, overview. It has two subdomains, the first six helices create the C1 subdomain and the last two helices, alpha7 and alpha8, create the C2 subdomain. The primase CTD is in the closed conformation, but NMR dynamic studies indicate there is considerable movement in the linker between the two subdomains and that N564 is the most dynamic residue within the linker Staphylococcus aureus

Synonyms

Synonyms Comment Organism
DnaG primase
-
 Staphylococcus aureus

General Information

General Information Comment Organism
evolution enzyme structure comparisons and phylogenetic analysis Staphylococcus aureus
additional information protein backbone dynamics by NMR Staphylococcus aureus
physiological function DnaG primase is stimulated by the homohexameric DnaB helicase, termed DnaC helicase in Staphylococcus aureus. DnaC helicase /DnaB helicase dissociates the two strands of duplex DNA during DNA replication while hydrolyzing ATP, and travels processively in the 5'-3' direction along the single-stranded lagging template toward the replication fork, communicating allosterically with the multi-subunit replicative DNA polymerase. This action keeps it in proximity of the replication fork and ensures the primers are synthesized on the exposed single-stranded DNA nearest to the replication fork. Since primase activity is weak, the stimulation by DnaB causes primase to synthesize primers only at the replication fork when and where they are needed Staphylococcus aureus