EC Number   |
Subunits |
Reference |
|---|
   3.1.30.2 | ? |
x * 43000, SDS-PAGE |
680576 |
| 3.1.30.2 | dimer |
homodimer, crystal structure analysis |
677620 |
| 3.1.30.2 | dimer |
monomer and dimer of the enzyme are catalytically active |
666881 |
| 3.1.30.2 | homodimer |
each monomer consists of 245 amino acids, they function independently of each other, monomer and dimer can function with same specific activity. Dimer form has an electrostatic advantage over the monomer to associate with DNA, inner-sphere binding in the monomer, outer-sphere in the dimer, interface of the protein and DNA is full of charged side chains, such as Arg57, Arg87, Arg125, Arg196, and Mg2+. Interfacial region is highly hydrated with an average of 27 hydration sites in the monomer (water acts more to screen the electrostatic region between the monomer and DNA) and 31 sites in the dimer (water acts more as a glue to provide structural adaptability with the protein and DNA). Dynamics of H-bonds of water in this active centre only little difference is found (water in the working region in the dimer complex has larger fluctuations than in monomer). Dimerization leads to different contacts between DNA and protein residues, especially to Mg2+ |
699775 |
| 3.1.30.2 | monomer |
1 * 33000, decarboxylated, SDS-PAGE |
95075 |
| 3.1.30.2 | monomer |
1 * 34000, SDS-PAGE |
666651 |
| 3.1.30.2 | monomer |
1 * 49000, SDS-PAGE, native mass by gel filtration |
678425 |
| 3.1.30.2 | monomer |
monomer and dimer of the enzyme are catalytically active |
666881 |
| 3.1.30.2 | More |
the subunits of the dimer function independently as monomers, molecular dynamic simulations, modelling of complex building with DNA, hydration sites of the enzyme depending on solvent density, overview |
666881 |
