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Literature summary for 5.6.1.7 extracted from

  • van Duijn, E.; Simmons, D.A.; van den Heuvel, R.H.; Bakkes, P.J.; van Heerikhuizen, H.; Heeren, R.M.; Robinson, C.V.; van der Vies, S.M.; Heck, A.J.
    Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring (2006), J. Am. Chem. Soc., 128, 4694-4702.
    View publication on PubMed
Search for more literature for 5.6.1.7

Organism

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information GroEL binds only one molecule of the model substrate Rubisco. In contrast, the capsid protein of bacteriophage T4, a natural GroEL substrate, can occupy both rings simultaneously. Each substrate induces distinct conformational changes in the GroEL chaperonin. Binding of Rubisco to the GroEL oligomer stabilizes the chaperonin complex significantly, whereas binding of one capsid protein does not have the same effect. Addition of a second capsid protein molecule to GroEL results in a similar stabilizing effect to that obtained after the binding of a single Rubisco. The binding of a single capsid polypeptide does not induce significant conformational changes in the GroEL trans ring, and hence the unoccupied GroEL ring remains accessible for a second capsid molecule Escherichia coli ?
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Synonyms

Synonyms Comment Organism
GroEL chaperonin
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 Escherichia coli