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Literature summary for 3.6.4.B10 extracted from

  • Nakagawa, A.; Moriya, K.; Arita, M.; Yamamoto, Y.; Kitamura, K.; Ishiguro, N.; Kanzaki, T.; Oka, T.; Makabe, K.; Kuwajima, K.; Yohda, M.
    Dissection of the ATP-dependent conformational change cycle of a group II chaperonin (2014), J. Mol. Biol., 426, 447-459.
    View publication on PubMed
Search for more literature for 3.6.4.B10

Protein Variants

Protein Variants Comment Organism
D64A/D393A site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change Thermococcus sp.
D64A/D393A/K485W site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview Thermococcus sp.
K485W site-directed mutagenesis, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview Thermococcus sp.
L265W site-directed mutagenesis, replacement of amino acid L265 with Trp partially impairs the protein folding activity, eight Trp residues are thought to come close in the closed conformation. The resulting steric hindrance might interrupt the conformational changes required for protein folding. Although ATP hydrolysis activity is almost completely lost in the absence of K+, slight ATP-dependent folding activity is observed Thermococcus sp.
L56W site-directed mutagenesis, the mutant exhibits nearly the same level of protein folding activity as the wild-type protein Thermococcus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis, stopped-flow fluorometry and stopped-flow small-angle X-ray scattering and ATP dissociation constants of wild-type and mutant enzymes. Allosteric communication in the group II chaperonins lies only in the intra-ring contact regions, which are located entirely within the equatorial domains. No cooperativity in ATP binding Thermococcus sp.

Metals/Ions

Metals/Ions Comment Organism Structure
K+ required, the ATP hydrolysis rate is negligible in the absence of K+ Thermococcus sp.
Mg2+ required 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
-
 ?

Organism

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

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
-
 ?

Synonyms

Synonyms Comment Organism
thermosome
-
 Thermococcus sp.
TKS1-CPN
-
 Thermococcus sp.

General Information

General Information Comment Organism
additional information reaction cycle model for group II chaperonins, ATP-binding, stopped-flow fluorometry and stopped-flow small-angle X-ray scattering, overview Thermococcus sp.
physiological function the group II chaperonin captures an unfolded protein while in its open conformation and then mediates the folding of the protein during ATP-driven conformational change cycle Thermococcus sp.