EC Number   |
Subunits |
Reference |
|---|
   3.6.4.13 | ? |
x * 100000, gel filtration |
692935 |
| 3.6.4.13 | ? |
x * 119037, calculated from sequence |
694416 |
| 3.6.4.13 | ? |
x * 49800, recombinant C-terminal helicase domain (amino-acid sequence corresponding to that between residues 189 and 620 of the predicted NS3 polypeptide), SDS-PAGE |
690244 |
| 3.6.4.13 | ? |
x * 56941, sequence calculation |
-, 756906 |
| 3.6.4.13 | ? |
x * 66000, recombinant NS3, SDS-PAGE, x * 109000, recombinant MBP-fusion NS3 protein, SDS-PAGE |
-, 697614 |
| 3.6.4.13 | ? |
x * 70000, His-tagged enzyme, SDS-PAGE |
693899 |
| 3.6.4.13 | dimer |
crystal structure, three-domain structure with asymmetric distribution of charges on the surface and a tunnel structure for RNA substrate access, overview |
670078 |
| 3.6.4.13 | dimer |
the helicase core of CsdA is comprised of two RecA-like domains (RecA1 and RecA2) joined by a flexible linker and contains all conserved motifs, two previously auxiliary domains are found: a dimerization domain (DD) and an RNA-binding domain (RBD), conformational flexibilities of the helicase core domains and C-terminal regions, enzyme domain structure, three-dimensional modelling, detailed overview. DD is indispensable for stabilizing the CsdA dimeric structure. Structure comparisons |
758485 |
| 3.6.4.13 | monomer |
1 * 130000, SDS-PAGE |
692932 |
| 3.6.4.13 | monomer |
alphabeta, 29% alpha-helix, 15% beta-sheet, and 56% non-regular structures, globular monomer accounts for 90%, a small percentage (7%) of dimers or trimers, higher oligomers almost absent (3%), analytical centrifugation and gel filtration |
-, 701395 |
