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Literature summary for 3.6.4.B10 extracted from

  • Yamamoto, Y.Y.; Abe, Y.; Moriya, K.; Arita, M.; Noguchi, K.; Ishii, N.; Sekiguchi, H.; Sasaki, Y.C.; Yohda, M.
    Inter-ring communication is dispensable in the reaction cycle of group II chaperonins (2014), J. Mol. Biol., 426, 2667-2678.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged wild-type and mutant enzyme oligomer rings in Escherichia coli Thermococcus sp.

Protein Variants

Protein Variants Comment Organism
K165A/K485W site-directed mutagenesis, ATPase inactive mutant that can partially prevent the spontaneous refolding ofGFP and refold it in an ATP-dependent manner Thermococcus sp.
K485W site-directed mutagenesis, the mutant shows ATP binding and conformational change upon ATP binding Thermococcus sp.
additional information construction of the asymmetric ring complex of a group II chaperonin using circular permutated covalent mutants, TKS1-CPNASR. Although one ring of the asymmetric ring complex lacks ATPase or ATP binding activity, the other wild-type ring undergoes an ATP-dependent conformational change and maintains protein-folding activity. It is possible to construct covalent chaperonin complexes by connecting N and C-termini. Circular permutated covalent enzyme TKS1-CPN (CPNCPC) is constructed by applying circular permutation to the covalent TKS1-CPN dimer, the circular permutated covalent TKS1-CPN dimer that has the deletion of 95 amino acids from its N-terminus and the addition of the same 95 amino acids to its C-terminus can assemble into a doublering structure similar to the wild-type. The 95th amino acid residue is located at the loop region between Helix 4 and Helix 5. The complex of the TKS1-CPN variant has ann molecular weight of approximately 120 kDa determined by SDS-PAGE. The ATPase activity of mutant CPNASR is half that of the recombinant His-tagged CPNwild-type homooligomer. Phenotypes, overview Thermococcus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Thermococcus sp.
-
ADP + phosphate
-
?
ATP + H2O Thermococcus sp. KS-1
-
ADP + phosphate
-
?
ATP + H2O Thermococcus sp. KS1
-
ADP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Thermococcus sp. O24730 beta-subunit
-
Thermococcus sp. P61112 alpha-subunit
-
Thermococcus sp. KS-1 O24730 beta-subunit
-
Thermococcus sp. KS1 P61112 alpha-subunit
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzyme oligomer rings from Escherichia coli Thermococcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Thermococcus sp. ADP + phosphate
-
?
ATP + H2O
-
Thermococcus sp. KS-1 ADP + phosphate
-
?
ATP + H2O
-
Thermococcus sp. KS1 ADP + phosphate
-
?
additional information enzyme TKS1-CPN shows a strong protein-folding activity Thermococcus sp. ?
-
?
additional information enzyme TKS1-CPN shows a strong protein-folding activity Thermococcus sp. KS-1 ?
-
?
additional information enzyme TKS1-CPN shows a strong protein-folding activity Thermococcus sp. KS1 ?
-
?

Synonyms

Synonyms Comment Organism
TKS1-CPN
-
Thermococcus sp.

General Information

General Information Comment Organism
additional information chaperonins are ubiquitous molecular chaperones with the subunit molecular mass of 60 kDa. They exist as double-ring oligomers with central cavities. An ATP-dependent conformational change of the cavity induces the folding of an unfolded protein that is captured in the cavity. Inter-ring communication is dispensable in the reaction cycle of group II chaperonins. Group II chaperonins do not require a co-chaperonin but have a built-in lid that is composed of a helical protrusion in the apical domain. The built-in lid seals off the central cavity and induces a conformational change to assist the folding of the trapped substrate, molecular mechanism analysis. Structure modeling of wild-type and mutant enzyme oligomers using structure of Thermococcus sp. JCM 11816, PDB ID 1Q2V, overview Thermococcus sp.
physiological function chaperonins are ubiquitous molecular chaperones performing an ATP-dependent conformational change of the cavity that induces the folding of an unfolded protein that is captured in the cavity Thermococcus sp.