Literature summary for 5.6.1.7 extracted from

Roseman, A.M.; Chen, S.; White, H.; Braig, K.; Saibil, H.R.
The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL (1996), Cell, 87, 241-251.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
frozen-hydrated GroEL complexes, 30A resolution, 7fold symmetry, two interring contacts per subunit, ATP turnover causes allosteric switching between the rings by altering the interring contacts	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Escherichia coli	5829	-

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	-	-	-

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	-	?

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Release 2023.1 (January 2023)