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Literature summary for 5.6.1.7 extracted from

  • Skjaerven, L.; Cuellar, J.; Martinez, A.; Valpuesta, J.M.
    Dynamics, flexibility, and allostery in molecular chaperonins (2015), FEBS Lett., 589, 2522-2532.
    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
-
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
-
?

Synonyms

Synonyms Comment Organism
GroEl
-
Escherichia coli

General Information

General Information Comment Organism
evolution the chaperonins are a family of molecular chaperones present in all three kingdoms of life. They are classified into group I and group II. Group I consists of the bacterial variants (GroEL) and the eukaryotic ones from mitochondria and chloroplasts (Hsp60). Both groups assemble into a dual ring structure, with each ring providing a protective folding chamber for nascent and denatured proteins Escherichia coli
additional information mechanisms and the structure-function relationships in the complex protein systems, structural dynamics, allostery, and associated conformational rearrangements, overview Escherichia coli
physiological function the chaperonin functional cycle is powered by ATP binding and hydrolysis, which drives a series of structural rearrangements that enable encapsulation and subsequent release of the substrate protein. Chaperonins have elaborate allosteric mechanisms to regulate their functional cycle. Long-range negative cooperativity between the two rings ensures alternation of the folding chambers. Positive intra-ring cooperativity, which facilitates concerted conformational transitions within the protein subunits of one ring, has only been demonstrated for group I chaperonins Escherichia coli