EC Number   |
Subunits |
Reference |
|---|
   3.4.21.53 | ? |
x * 77000, recombinant His-tagged Lon-like-Ms, SDS-PAGE |
-, 752612 |
| 3.4.21.53 | ? |
x * 83000, recombinant enzyme, SDS-PAGE |
753692 |
| 3.4.21.53 | ? |
x * 84269, calculated |
-, 718085 |
| 3.4.21.53 | ? |
x * 88800, calculated |
-, 718113 |
| 3.4.21.53 | ? |
x * 89000, Lon, SDS-PAGE |
692861 |
| 3.4.21.53 | ? |
x * 90000, SDS-PAGE |
-, 669251 |
| 3.4.21.53 | ? |
x * 90700, calculated and SDS-PAGE |
710400 |
| 3.4.21.53 | dimer |
- |
682726 |
| 3.4.21.53 | dodecamer |
hexamers of Escherichia coli Lon also interact to form a dodecamer at physiological protein concentrations, the dodecamer shows a prolate structure with the protease chambers at the distal ends and a matrix of N domains forming an equatorial hexamer-hexamer interface, with portals of about 45 A providing access to the enzyme lumen |
732825 |
| 3.4.21.53 | dodecamer |
the larger assembly has decreased ATPase activity and displays substrate-specific alterations in degradation compared to the hexamer. The enzyme dodecamer successfully completes many of the Lon protease's important regulatory functions while modifying substrate choice, perhaps to better manage protein quality control under conditions such as UV, heat, and oxidative stress. Identification of N domain interactions underlying Lon dodecamer formation. The Lon N domains are primarily responsible for dodecamer formation, the Lon dodecamer forms via putative N domain coiled-coil interactions. Analytical ultracentrifugation |
755340 |
