Literature summary for 3.4.21.92 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
A153P	crystallization data, disruption of handle region resulting in an altered ring-ring dimerization interface	Streptococcus pneumoniae

Organism

Organism	UniProt	Comment	Textmining
Streptococcus pneumoniae	-	-	-

Subunits

Subunits	Comment	Organism
More	there exists a flexible N-terminal loop in each enzyme subunit that is important for complex formation with ClpXP and ClpAP	Streptococcus pneumoniae

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Release 2023.1 (January 2023)