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Literature summary for 5.6.1.7 extracted from

  • Hayer-Hartl, M.; Bracher, A.; Hartl, F.U.
    The GroEL-GroES chaperonin machine: a nano-cage for protein folding (2016), Trends Biochem. Sci., 41, 62-76.
    View publication on PubMed

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
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ADP + phosphate + an unfolded polypeptide
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additional information Escherichia coli the GroEL/ES system promotes protein folding, mechanism overview ?
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide reaction mechanism of the enzyme complex, the asymmetric and symmetric GroEL/ES interaction cycles in the presence of substrate protein, respectively, substrate binding in passive cage model and active cage model, detailed overview Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide
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Escherichia coli ADP + phosphate + an unfolded polypeptide
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ATP + H2O + a folded polypeptide GroEL, non-native protein, and GroES undergo ATP-regulated binding and release cycles Escherichia coli ADP + phosphate + an unfolded polypeptide
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additional information the GroEL/ES system promotes protein folding, mechanism overview Escherichia coli ?
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additional information the apical GroEL domain (residues 191-376) binds cofactor non-native substrate protein, helices H (residues 233-243) and I (residues 255-267) of the apical domains expose multiple hydrophobic amino acids towards the ring center, forming a circular surface for the binding of a non- native substrate protein, GroEL/ES cycling in the presence of substrate, overview. The C-terminal Gly-Gly-Met repeat sequences are also required for accelerated folding Escherichia coli ?
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Subunits

Subunits Comment Organism
tetradecamer like all group I chaperonins, GroEL of Escherichia coli is a cylindrical complex of two heptameric rings of about 57 kDa subunits. The subunits are composed of three domains formed by discontinuous sequence elements, an equatorial ATP-binding domain (residues6-133, 409-523), an intermediate hinge domain (residues134-190, 377-408), and an apical domain (residues191-376) that binds cofactors non-native SP and GroES Escherichia coli

Synonyms

Synonyms Comment Organism
GroEl
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
GroES the GroEL-GroES chaperonin machine is a nano-cage for protein folding, the apical GroEL domain (residues191-376) binds cofactor GroES. GroES is a dome-shaped heptameric ring of about 10 kDa subunits, binds to the ends of the GroEL cylinder, forming the cage in which the substrate protein is encapsulated for folding Escherichia coli

General Information

General Information Comment Organism
evolution the bacterial chaperonin GroEL, with its lid-like cofactor GroES, is the archetypical member of the class of protein folding machines. GroEL belongs to the chaperonins of group I, which are found in bacteria as well as in mitochondria and chloroplasts, the eukaryotic organelles that descend from bacterial endosymbionts Escherichia coli
malfunction a wider range of newly synthesized proteins aggregated upon rapid loss of GroEL function in a temperature-sensitive GroEL mutant strain. Most GroEL interactors are 35-60 kDa in size, consistent with the volume of the GroEL-GroES cavity. Role of chaperonin in evolution, overview Escherichia coli
additional information cavity closure is triggered by ATP binding Escherichia coli
physiological function the GroEL-GroES chaperonin machine is a nano-cage for protein folding. GroEL, non-native protein, and GroES undergo ATP-regulated binding and release cycles. GroEL/ES is required for Escherichia coli growth under all conditions, indicating the existence of essential proteins that depend on the chaperonin for folding. While GroEL interacts with a wide range of denatured proteins in vitro, only a limited set of 250 proteins bind stably to GroEL upon translation in vivo, corresponding to about 10% of total Escherichia coli cytosolic proteins and including 67 essential proteins Escherichia coli