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Literature summary for 5.6.1.7 extracted from

  • Kim, S.Y.; Miller, E.J.; Frydman, J.; Moerner, W.E.
    Action of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET (2010), J. Mol. Biol., 401, 553-563.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide folding of the model substrate Hippel–Lindau tumor suppressor protein VHL in an ATP-dependent manner. Heterogeneity of the action of GroES/EL on a bound polypeptide substrate might arise from the random nature of the specific binding to the various identical subunits of GroEL, and might help explain why multiple rounds of binding and hydrolysis are required for some chaperonin substrates Escherichia coli ADP + phosphate + an unfolded polypeptide
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Synonyms

Synonyms Comment Organism
chaperonin GroEL/ES
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
GroES cofactor. ATP- and GroES-induced confinement within the GroEL cavity remodels bound polypeptides by causing expansion (or racking) of some regions and compaction of others, most notably, the hydrophobic core Escherichia coli

General Information

General Information Comment Organism
physiological function the double ring-shaped chaperonin GroEL binds a wide range of non-native polypeptides within its central cavity and, together with its cofactor GroES, assists their folding in an ATP-dependent manner Escherichia coli