EC Number   |
Subunits |
Reference |
|---|
   3.4.21.B30 | homodimer |
- |
718023 |
| 3.4.21.B30 | homodimer |
2 * 15000, recombinant enzyme UmuD, SDS-PAGE |
731823 |
| 3.4.21.B30 | dimer |
2 * 15063 |
668783 |
| 3.4.21.B30 | homodimer |
2 * 15500, predicted from amino acid sequence |
682581 |
| 3.4.21.B30 | dimer |
although UmuD and UmuD' form homodimers, they preferentially form heterodimers, crosslinking experiments, SDS-PAGE |
653604 |
| 3.4.21.B30 | dimer |
although UmuD and UmuD' form homodimers, they preferentially form heterodimers, SDS-PAGE |
650976 |
| 3.4.21.B30 | dimer |
crystallization experiments |
653917 |
| 3.4.21.B30 | dimer |
enzyme can form homodimers, crosslinking experiments, SDS-PAGE |
651622, 651630 |
| 3.4.21.B30 | More |
in addition to forming molecular dimers, the N-and C-terminal tails of UmuD' extend from a globular beta structure to associate and produce crystallized filaments. Higher oligomers are found in solution with UmuD' but not with UmuD nor with a mutant of UmuD' lacking the extended N terminus |
653917 |
| 3.4.21.B30 | tetramer |
two dimers form a tetramer, wild-type and V34C mutant, SDS-PAGE |
651628 |
