Literature summary extracted from
Gribun, A.; Kimber, M.S.; Ching, R.; Sprangers, R.; Fiebig, K.M.; Houry, W.A.
The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation (2005), J. Biol. Chem., 280, 16185-16196.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.4.21.92 |
mutant A153P, disruption of handle region resulting in an altered ring-ring dimerization interface. There exists a flexible N-terminal loop in each enzyme subunit that is important for complex formation with ClpXP and ClpAP |
Streptococcus pneumoniae |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.4.21.92 |
A153P |
crystallization data, disruption of handle region resulting in an altered ring-ring dimerization interface |
Streptococcus pneumoniae |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.21.92 |
Streptococcus pneumoniae |
- |
- |
- |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.4.21.92 |
More |
there exists a flexible N-terminal loop in each enzyme subunit that is important for complex formation with ClpXP and ClpAP |
Streptococcus pneumoniae |