EC Number   |
Subunits |
Reference |
|---|
   3.6.4.6 | ? |
x * 50000, SDS-PAGE |
758466 |
| 3.6.4.6 | decamer |
mutants Vps4pE233Q and Vps4pdeltaCC/E233Q, SDS-PAGE |
210582 |
| 3.6.4.6 | dimer |
2 * 42248, calculated from sequence, the enzyme rapidly interconverts between multiple oligomeric states, it interconverts between dimers and hexamers in the presence of adenosine nucleotides |
-, 725724 |
| 3.6.4.6 | dimer |
SDS-PAGE |
210582 |
| 3.6.4.6 | dimer |
the enzyme interconverts between dimers and hexamers in the presence of adenosine nucleotides |
725724 |
| 3.6.4.6 | dimer |
Vps4p dimers form two distinct heptameric rings and accommodate AAA cassettes in a head-to-head fashion, X-ray crystallography |
699526 |
| 3.6.4.6 | dodecamer |
- |
699527 |
| 3.6.4.6 | hexamer |
- |
688690, 733702, 756027 |
| 3.6.4.6 | hexamer |
3D structures of NSF in its functional cycle are reconstructed: NSF in the ATP state, which is capable of binding substrates, the 20S particle, consisting of the NSF hexamer, three alpha-SNAPs and the SNARE complex and NSF in the ADP state. These structures reveal that the two AAA+ domains of NSF, D1 and D2, are in a parallel arrangement in the full-length NSF hexamer, similarly to p97, as shown in its full-length hexamer crystal structures |
720534 |
| 3.6.4.6 | hexamer |
6 * 42248, calculated from sequence, the enzyme rapidly interconverts between multiple oligomeric states, it interconverts between dimers and hexamers in the presence of adenosine nucleotides |
-, 725724 |
