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Literature summary for 3.6.4.10 extracted from
- Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB (2007), Mol. Cell, 25, 261-271.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Thermus thermophilus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| electron cryomicroscopy reconstruction of ATP-activated trap mutant E271A/E668A, along with native ClpB, in complex with ADP or 5'-adenylyl-beta,gamma-imidodiphosphate, or nucleotide-free. Motif 2 of the ClpB domain M is positioned between the D1-large domains of neighboring subunits and could facilitate a concerted, ATP-driven conformational change in the AAA-1 ring. ATP is essential for high-affinity substrate binding to ClpB and cannot be substituted by 5'-adenylyl-beta,gamma-imidodiphosphate | Thermus thermophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E271A/E668A | trap mutant, electron cryomicroscopy reconstruction | Thermus thermophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | - |
isoform ClpB | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + H2O = ADP + phosphate | ClpB captures substrates on the upper surface of the AAA-1 ring before threading them through the ClpB hexamer in an ATP hydrolysis-driven step | Thermus thermophilus |
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