EC Number   |
Subunits |
Reference |
|---|
   3.1.26.11 | ? |
- |
441624 |
| 3.1.26.11 | ? |
x * 43000, mitochondrial RNase Z, SDS-PAGE |
441609 |
| 3.1.26.11 | ? |
x * 45000, SDS-PAGE |
441624 |
| 3.1.26.11 | dimer |
- |
678248 |
| 3.1.26.11 | dimer |
cross-linking, SDS-PAGE |
665663 |
| 3.1.26.11 | dimer |
crystallization |
665611 |
| 3.1.26.11 | dimer |
crystallization, active site located near the dimer interface, flexible arm clamping the tRNA protrudes from the core into solution |
677382 |
| 3.1.26.11 | dimer |
gel filtration analysis shows that, only 20% of tRNase Z2 molecules form dimers, while tRNase Z molecules exist as dimers. This inefficient tRNase Z2 dimer formation may be attributed to the lack of alpha1, alpha2, and alpha3 that are important for dimerization of tRNase Z |
-, 746960 |
| 3.1.26.11 | dimer |
homodimer, crystal structure |
665404, 666439 |
| 3.1.26.11 | homodimer |
- |
690641 |
