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Literature summary for 3.6.4.B10 extracted from

  • Jayasinghe, M.; Shrestha, P.; Wu, X.; Tehver, R.; Stan, G.
    Weak intra-ring allosteric communications of the archaeal chaperonin thermosome revealed by normal mode analysis (2012), Biophys. J., 103, 1285-1295.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.B10

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Thermoplasma acidophilum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Thermoplasma acidophilum
-
 ADP + phosphate
-
 ?
ATP + H2O Thermoplasma acidophilum ATCC 25905
-
 ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Thermoplasma acidophilum P48424 alpha-subunit
-
Thermoplasma acidophilum P48425 beta-subunit
-
Thermoplasma acidophilum ATCC 25905 P48424 alpha-subunit
-
Thermoplasma acidophilum ATCC 25905 P48425 beta-subunit
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Thermoplasma acidophilum ADP + phosphate
-
 ?
ATP + H2O
-
 Thermoplasma acidophilum ATCC 25905 ADP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
thermosome
-
 Thermoplasma acidophilum

General Information

General Information Comment Organism
evolution the enzyme belongs to the group II chaperonins, which are found in archaeal (thermosome of Thermoplasma acidophilum) and in eukaryotic (chaperonin-containing TCP-1 or CCT) species, have eight or nine subunits per ring made of two (thermosome) or eight (CCT) types of subunits. Subunit heterogeneity in group II chaperonins, found primarily within the apical domains, has important consequences for the functional specialization of ring components, role of heterogeneity in subunit dynamics. Nonconservation of intra-ring cooperativity among chaperonin classes, overview Thermoplasma acidophilum
additional information three-dimensional structures of nucleotide states of thermosome and allosteric communications within the archaeal chaperonin thermosome, open and closed states and transitional conformation changes, computational analysis, overview Thermoplasma acidophilum
physiological function chaperonins are molecular machines that use ATP-driven cycles to assist misfolded substrate proteins to reach the native state. During the functional cycle, these machines adopt distinct nucleotide-dependent conformational states, which reflect large-scale allosteric changes in individual subunits. Archaeal and eukaryotic chaperonins undergo sequential subunit motions, analysis of the mode of action and mechanism. The thermosome double-ring structure has large contribution from higher-frequency modes Thermoplasma acidophilum