Literature summary for 3.6.4.10 extracted from

Aguado, A.; Fernandez-Higuero, J.A.; Cabrera, Y.; Moro, F.; Muga, A.
ClpB dynamics is driven by its ATPase cycle and regulated by the DnaK system and substrate proteins (2015), Biochem. J., 466, 561-570.

Search for more literature for 3.6.4.10

Activating Compound

Activating Compound	Comment	Organism	Structure
alpha-casein	-	Plasmodium falciparum
additional information	deletion of the N-terminal domain activates the basal activity 2fold, whereas elimination of the M domain increases the ATPase activity 10fold in the presence of casein	Plasmodium falciparum

Protein Variants

Protein Variants	Comment	Organism
E371C	site-directed mutagenesis, the chaperone activity of ClpBE731C is similar to that of the wild-type protein	Plasmodium falciparum
additional information	deletion of the N-terminal domain activates the basal activity 2fold, whereas elimination of the M domain increases the ATPase activity 10fold in the presence of casein. Attachment of fluorescent probes in the M domain and NBD2 does not affect the activity of ClpBS433C, it decreases that of ClpBE731C, especially when labelled with Alexa Fluor 350 (3fold reduction), and severely inhibits the ClpBS499C variant, overview	Plasmodium falciparum
S433C	site-directed mutagenesis, the chaperone activity of ClpBS433C is similar to that of the wild-type protein	Plasmodium falciparum
S499C	site-directed mutagenesis, the mutant shows 10-20fold increased ATPase activity, the chaperone activity of mutantt ClpBS499C is 20-25% more efficient than the wild-type	Plasmodium falciparum

General Stability

General Stability	Organism
ATP binding to ClpB stabilizes the enzyme hexamer and ADP dissociates it	Plasmodium falciparum

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
apicoplast	-	Plasmodium falciparum	20011	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Plasmodium falciparum	-	ADP + phosphate	-	?
additional information	Plasmodium falciparum	association between ClpB and DnaK at the protein aggregate surface, the substrate-binding domain of DnaK regulates ClpB dynamics	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Plasmodium falciparum	Q8IB03	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Plasmodium falciparum	ADP + phosphate	-	?
additional information	association between ClpB and DnaK at the protein aggregate surface, the substrate-binding domain of DnaK regulates ClpB dynamics	Plasmodium falciparum	?	-	?

Subunits

Subunits	Comment	Organism
homohexamer	each monomer contains four domains, an N-terminal domain, two nucleotide-binding domains (NBD1 and NBD2), and a middle (M) domain. The M domain, which is specific for ClpB and its homologues, is inserted into the NBD1, folds as a coiled-coil structure built up by four helices. ATP binding to ClpB stabilizes the protein hexamer and ADP dissociates it	Plasmodium falciparum

Synonyms

Synonyms	Comment	Organism
ClpB	-	Plasmodium falciparum
PfClpB1	-	Plasmodium falciparum

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	30	assay at	Plasmodium falciparum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Plasmodium falciparum

General Information

General Information	Comment	Organism
additional information	each monomer of the hexameric enzyme containing four domains: an N-terminal domain, which improves the reactivation efficiency of stable protein aggregates, connected to the rest of the protein by a conserved linker, two nucleotide-binding domains (NBD1 and NBD2) that bind and hydrolyse ATP, and a middle (M) domain. The M domain, which is specific for ClpB and its homologues, is inserted into the NBD1, folds as a coiled-coil structure built up by four helices and is strictly required for the disaggregase activity of the chaperone. ClpB dynamics is modulated by the DnaK system and substrate proteins, effect of the N-terminal and M domains on ClpB dynamics, overview. The substrate-binding domain of DnaK regulates ClpB dynamics	Plasmodium falciparum

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Release 2023.1 (January 2023)