Literature summary extracted from
Lee, S.; Choi, J.M.; Tsai, F.T.
Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB (2007), Mol. Cell, 25, 261-271.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.6.4.10 |
expression in Escherichia coli |
Thermus thermophilus |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.6.4.10 |
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
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.6.4.10 |
E271A/E668A |
trap mutant, electron cryomicroscopy reconstruction |
Thermus thermophilus |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.6.4.10 |
Thermus thermophilus |
- |
isoform ClpB |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
3.6.4.10 |
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 |
|