EC Number   |
|---|
   2.7.7.102 | - |
| 2.7.7.102 | crystal structure in complex with UTP. The primase binds the triphosphate moiety of the UTP at the active site, which includes residues Asp95, Asp97, and Asp280, essential for the nucleotidyl transfer reaction. Construction of a model between the DNA primase and a primer/template DNA for the primer synthesis |
| 2.7.7.102 | N-terminal domain (NTD) of PriL, residues 1-222 that bind to small subunit PriS at 2.9 A resolution. The PriL-NTD structure consists of the helix-bundle and twisted-strand domains. The conserved hydrophobic Tyr155-Tyr156-Ile157 region near the flexible region is the PriS-binding site |
| 2.7.7.102 | native and selenomethionine-substituted protein, to 1.8 and 2.2 A resolution, respectively, space group P3(2)21 |
| 2.7.7.102 | primase domain, hanging drop vapour diffusion technique |
| 2.7.7.102 | strcuture of the highly conserved C-terminal regulatory domain of the large subunit to 1.7 A resolution. The evolutionarily conserved 4Fe-4S cluster is buried deeply within the protein core. DNA binding shows a strong preference for ss/dsDNA junction substrates. The enzyme interacts specifically with the C-terminal domain of the intermediate subunit of replication protein A, RPA32C |
| 2.7.7.102 | structure of small subunit Prim1 at 2.2 A resolution, with citrate in its inactive forms. Dibasic citrate is bound at the nucleotide triphosphate beta, gamma-phosphate binding site through nine hydrogen bonds. The activity of Prim1 is regulated by pH and citrate |
| 2.7.7.102 | structure of the catalytic subunit, with bound UTP and Mn2+. Primase contains the conserved catalytic prim fold domain, with a subdomain different from the archaeal and bacterial primases. Residues S160 and H166 are in direct contact with UTP |
| 2.7.7.102 | structure of the complex Prim1/Prim2, at 2.65 A resolution, and modeling of the protein in complex with NTP and DNA/RNA substrates |
| 2.7.7.102 | vapour diffusion in sitting drops at 19°C. X-ray crystal structure of heterotrimeric PriSLX from S. solfataricus at 2.9 A resolution |
