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Literature summary for 5.6.1.7 extracted from

  • Dalton, K.M.; Frydman, J.; Pande, V.S.
    The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation (2015), PLoS ONE, 10, e0117724.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.7

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of crystal structures of the GroE chaperonin from Escherichia coli in the open, ATP-bound, PDB ID 1KP8, and closed, PDB ID 1AON, states Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + a folded polypeptide Escherichia coli
-
 ADP + phosphate + an unfolded polypeptide
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide enzyme reaction mechanism and the mechanism by which the C-terminus influences the activity of GroEL, structure-function relationship, overview Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide
-
 Escherichia coli ADP + phosphate + an unfolded polypeptide
-
 ?

Subunits

Subunits Comment Organism
tetradecamer GroE consists of the GroEL complex, an (alpha7)2 homoligomer with a dual-ring topology, and its homoheptameric cofactor, GroES Escherichia coli

Synonyms

Synonyms Comment Organism
GroEl
-
 Escherichia coli
group I chaperonin
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
GroES GroE consists of the GroEL complex, an (alpha7)2 homoligomer with a dual-ring topology, and its homoheptameric cofactor, GroES, which acts as a lid for the GroEL folding chamber Escherichia coli

General Information

General Information Comment Organism
additional information chaperonins are large ring shaped oligomers that facilitate protein folding by encapsulation within a central cavity. All chaperonins possess flexible C-termini which protrude from the equatorial domain of each subunit into the central cavity. The termini play an important role in the allosteric regulation of the ATPase cycle, in substrate folding and in complex assembly and stability, the termini undergo a heretofore unappreciated conformational cycle which is coupled to the nucleotide state of the enzyme, localization of the termini throughout the nucleotide cycle of the group I chaperonin GroE, molecular dynamics simulations, overview. GroE consists of the GroEL complex, an (alpha7)2 homoligomer with a dual-ring topology, and its homoheptameric cofactor, GroES, which acts as a lid for the GroEL folding chamber Escherichia coli