EC Number   |
Subunits |
Reference |
|---|
   2.7.7.101 | ? |
x * 60000, SDS-PAGE |
751002 |
| 2.7.7.101 | monomer |
1 * 68800, calculated from sequence, 1 * 69000, SDS-PAGE |
750533 |
| 2.7.7.101 | More |
an N-terminal zinc-binding domain (ZBD) responsible for DNA template recognition, a central catalytic domain (RNA polymerase domain, RPD), and a C-terminal helicase-binding domain (HBD or DnaGC), which is responsible for interaction with DnaB helicase and single-stranded DNA-binding protein (SSB) |
760348 |
| 2.7.7.101 | More |
archaeal DnaG contains N- and C-terminal domains flanking a TOPRIM domain. The N-terminal domain is a RNA-binding domain with poly(rA)-preference cooperating with the TOPRIM domain in binding of RNA |
739191 |
| 2.7.7.101 | 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 |
760945 |
| 2.7.7.101 | 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 |
760588 |
| 2.7.7.101 | More |
in a crystal structure of the Geobacillus stearothermophilus DnaB6-(DnaGC)3 complex, the three C-terminal domains of primase each bind to two adjacent subunits of the dilated N-tier of DnaB |
761889 |
| 2.7.7.101 | More |
MtDnaG-CTD interacts at the dimer-dimer interface of MtDnaB-NTD using mostly hydrophobic residues of the helical hairpin regions (HHRs). The dimer-dimer interface of MtDnaB-NTD is considered as a DnaG-binding site |
-, 760530 |
