EC Number   |
Subunits |
Reference |
|---|
  3.4.21.B50 | dodecamer |
12 * 48000-50000, dynamic light-scattering, DegQ assembles into large, cage-like dodecamers that form independently of unfolded substrate proteins. Dodecamer-formation is essential for the degradation of substrate proteins but not for the chaperone activity of DegQ |
718323 |
| 3.4.21.B50 | dodecamer |
12 * 50000, SDS-PAGE |
651624 |
| 3.4.21.B50 | dodecamer |
substrate-containing form, 12 * 50000, SDS-PAGE |
718408 |
| 3.4.21.B50 | hexamer |
6 * 50000, SDS-PAGE |
651624 |
| 3.4.21.B50 | hexamer or dodecamer |
hexameric structure of mature enzyme, the Deg2 hexamer exists predominantly during substrate incubation in a resting state,the large oligomeric state is the active state, model of oligomeric state change, overview |
732074 |
| 3.4.21.B50 | More |
DegQLp forms predominantly trimers in the substrate-free state. In vitro, oligomerization is influenced by the pH of the protein solution and the presence of co-purified peptides binding to the PDZ1 and/or protease site. Misfolded proteins or peptides promote the assembly of protease active 12- or 24-mers the assembly of proteolytically active |
-, 754420 |
| 3.4.21.B50 | More |
structure-function analysis of the dimerization interface between Deg2 trimers, overview. The enzyme contains a unique second PDZ domain (PDZ2) following a conventional PDZ domain (PDZ1), with PDZ2 orchestrating the cage assembly of the enzyme, a conserved internal ligand for PDZ2 mediates hexamer formation and locks the protease in the resting state. Because loop JK lies outside the hexamer shell, it provides protection for the loop LA-PDZ2 interface from solvents and may play a role in changes in the oligomeric enzyme state |
732074 |
| 3.4.21.B50 | trimer |
substrate-free form |
718408 |
