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Literature summary for 3.6.4.10 extracted from

  • Yamasaki, T.; Oohata, Y.; Nakamura, T.; Watanabe, Y.H.
    Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement (2015), J. Biol. Chem., 290, 9789-9800.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
E271Q/R576C/A821C site-directed mutagenesis Thermus thermophilus
E271Q/R576C/E668Q/A821C site-directed mutagenesis Thermus thermophilus
K204A/T205A/R576C/A821C site-directed mutagenesis Thermus thermophilus
K204A/T205A/R576C/K601A/K602A/A821C site-directed mutagenesis Thermus thermophilus
additional information preparation of ordered heterohexamers of ClpB from Thermus thermophilus, in which two subunits having different mutations were cross-linked to each other and arranged alternately. ATPase activities of ordered heterohexamers with varyying mutations in the Walker A and B motifs, or the Arg-finger, of the two D domains, overview Thermus thermophilus
Q184C/A390C site-directed mutagenesis Thermus thermophilus
Q184C/A390C/E668Q site-directed mutagenesis Thermus thermophilus
Q184C/A390C/K601A/K602A site-directed mutagenesis Thermus thermophilus
Q184C/A390C/R747A site-directed mutagenesis Thermus thermophilus
Q184C/E271Q/A390C site-directed mutagenesis Thermus thermophilus
Q184C/E271Q/A390C/E668Q site-directed mutagenesis Thermus thermophilus
Q184C/K204A/T205A/A390C site-directed mutagenesis Thermus thermophilus
Q184C/K204A/T205A/A390C/K601A/K602A site-directed mutagenesis Thermus thermophilus
Q184C/R322A/A390C site-directed mutagenesis Thermus thermophilus
R322A/R576C/A821C site-directed mutagenesis Thermus thermophilus
R576C/A821C site-directed mutagenesis Thermus thermophilus
R576C/E668Q/A821C site-directed mutagenesis Thermus thermophilus
R576C/K601A/K602A/A821C site-directed mutagenesis Thermus thermophilus
R576C/R747A/A821C site-directed mutagenesis Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Thermus thermophilus
-
ADP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q9RA63
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Thermus thermophilus ADP + phosphate
-
?

Subunits

Subunits Comment Organism
heterohexamer a ring-shaped ClpB hexamer Thermus thermophilus

Synonyms

Synonyms Comment Organism
AAA+ chaperone ClpB
-
Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
protein aggregate reactivation assay at Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Thermus thermophilus

General Information

General Information Comment Organism
malfunction intercalation of ATPase defective subunits into the hexamer every other subunit hampers its ATPase and disaggregation activities Thermus thermophilus
additional information the ATPase cycle of ClpB proceeded as follows: (i) the 12 AAA+ modules randomly bound ATP, (ii) the binding of four or more ATP to one AAA+ ring is sensed by a conserved Arg residue and converted another AAA+ ring into the ATPase-active form, and (iii) ATP hydrolysis occurred cooperatively in each ring. Protein disaggregation activities of wild-type and cross-linked enzyme TClpB in cooperation with TDnaK system Thermus thermophilus
physiological function the ClpB hexamer hydrolyzes ATP and reactivates protein aggregates. ClpB cooperatively hydrolyzes ATP, and this cooperativity is crucial for protein disaggregation. Subunit D1 and D2 dimers have the essential properties of TClpB, evaluation of intersubunit cooperativity, overview Thermus thermophilus