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Literature summary for 3.6.4.B10 extracted from

  • Cong, Y.; Schroeder, G.; Meyer, A.; Jakana, J.; Ma, B.; Dougherty, M.; Schmid, M.; Reissmann, S.; Levitt, M.; Ludtke, S.; Frydman, J.; Chiu, W.
    Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle (2012), EMBO J., 31, 720-730.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.B10

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Bos taurus 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Bos taurus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
testis
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Bos taurus ADP + phosphate
-
 ?
ATP + H2O enzyme conformational changes upon ATP binding and throughout the ATPase cycle, structure-function relationship, overview Bos taurus ADP + phosphate
-
 ?

Subunits

Subunits Comment Organism
octamer unique asymmetric pattern among the eight subunits of TRiC in the nucleotide-free state, mechanism of TRiC negative inter-ring cooperativity. The TRiC lid remains open in three states of the cycle: ATP bound, ADP bound, and nucleotide free, structure-function relationship, structure modeling and electron cryo-microscopy, overview Bos taurus

Synonyms

Synonyms Comment Organism
chaperonin TRiC
-
 Bos taurus
eukaryotic group II chaperonin
-
 Bos taurus
TRiC/CCT
-
 Bos taurus

General Information

General Information Comment Organism
additional information ATP hydrolysis enhances the intra-ring TRiC subunit interactions, asymmetrically closed conformation of TRiC and expansion of the folding chambers in the ATP hydrolysis transition state, and chamber closing mechanisms of TRiC, structure modeling, overview. Mechanism of TRiC negative inter-ring cooperativity. The TRiC lid remains open in three states of the cycle: ATP bound, ADP bound, and nucleotide free Bos taurus