EC Number |
Subunits |
Reference |
---|
3.4.25.2 | ? |
x * 19000, HslV protein, SDS-PAGE |
647872 |
3.4.25.2 | ? |
x * 19095, calculation from nucleotide sequence |
647870 |
3.4.25.2 | dimer |
wild-type enzyme |
666429 |
3.4.25.2 | dodecamer |
- |
733478 |
3.4.25.2 | dodecamer |
12 * 23500, calculated from amino acid sequence |
-, 734007 |
3.4.25.2 | dodecamer |
HslV protease component |
735185 |
3.4.25.2 | dodecamer |
HslV, the proteolytic active sites are sequestered in the inner chamber of HslV |
665631 |
3.4.25.2 | dodecamer |
HslVU, a two-component proteasome-related prokaryotic system is composed of HslV protease and HslU ATPase. HslV protomers assemble in a dodecamer of two-stacked hexameric rings that form a complex with HslU hexamers. Structural analyses of protomer interfaces in HslV dodecamer suggests that HslV interfaces involve extensive area in which major determinants for function and stability constitute hot spots |
689884 |
3.4.25.2 | dodecamer |
HslVU, a two-component proteasome-related prokaryotic system is composed of HslV protease and HslU ATPase. HslV protomers assemble in a dodecamer of two-stacked hexameric rings that form a complex with HslU hexamers. Structural analysis of protomer interfaces in HslV dodecamer suggests that HslV interfaces involve extensive area in which major determinants for function and stability constitute hot spots |
689884 |
3.4.25.2 | hexamer |
HslU |
665631 |