EC Number   |
|---|
   2.7.7.101 | crystal structures of noncovalent DnaG-DNA complexes, of the RNA polymerase domain of DnaG and various DNA ligands. A key site for DnaG interaction with ds/ss DNA, located on the N-terminal subdomain of the RNAS polymerase domain |
| 2.7.7.101 | purified recombinant C-terminal domain of DnaG, mixing of 0.002 ml of 6 mg/ml native MtDnaG-CTD and 5 mg/ml selenomethionine-labeled MtDnaG-CTD with 0.002 ml of reservoir solution containing 20% w/v PEG 3350, 0.2 M magnesium acetate tetrahydrate, and equilibration against 0.5 ml of reservoir solution, for the SeMet-labeled protein a reeservoir solution of reservoir solution of 18% w/v PEG 3350, 0.15 M magnesium acetate, and MOPS, pH 7.6, is used, 4°C, 1-2 weeks, X-ray diffraction structure determination and analysis at 1.57-1.58 A resolution, modeling |
| 2.7.7.101 | structure of the RNA polymerase domain of DnaG. The tethered zinc binding domain plays an important role in the interactions between primase and specific template sequence. The ssDNA template binding surface is L-shaped, a model for the template ssDNA binding to primase is proposed. Comparison with the enzyme from Geobacillus stearothermophilus |
| 2.7.7.101 | structures of hexameric helicase DnaB and its complex with the helicase binding domain of DnaG. Within the hexamer the two domains of DnaB pack with different symmetries to form a distinct two-layered ring structure. Each of three bound DnaG helicase binding domains stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and guide the DNA to a DnaG active site |
| 2.7.7.101 | structures of the DnaG catalytic core bound to metal ion cofactors and either individual nucleoside triphosphates or the nucleotidyl alarmones, pppGpp and ppGpp |
