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Literature summary for 5.6.1.7 extracted from

  • Grason, J.P.; Gresham, J.S.; Lorimer, G.H.
    Setting the chaperonin timer: a two-stroke, two-speed, protein machine (2008), Proc. Natl. Acad. Sci. USA, 105, 17339-17344.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.7

Activating Compound

Activating Compound Comment Organism Structure
additional information conformational state allosteric interactions control speed of chaperonin cycle Escherichia coli
unfolded substrate protein chaperonin machine enhances hemicycle time and mean residence time set by the rate of ATP hydrolysis by the cis ring Escherichia coli

Protein Variants

Protein Variants Comment Organism
E315C mutant of GroEL Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli JM105
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a folded polypeptide high affinity in taut state Escherichia coli ADP + phosphate + an unfolded polypeptide
-
 ?
ATP + H2O + a folded polypeptide high affinity in taut state Escherichia coli JM105 ADP + phosphate + an unfolded polypeptide
-
 ?

Synonyms

Synonyms Comment Organism
GroEl relaxed state and taut state Escherichia coli
GroES
-
 Escherichia coli