FEATURES

FAMILY

DESCRIPTION

Also known as CH60_ECOLI, groEL, groL, mopA. Together with its co-chaperonin GroES, plays an essential role in assisting protein folding (PubMed:2897629, PubMed:2573517, PubMed:10532860, PubMed:1676490, PubMed:8104102, PubMed:9285593, PubMed:16751100, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391). The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding, probably by preventing aggregation and by entropically destabilizing folding intermediates (PubMed:16751100, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391). Rapid binding of ATP, followed by slower binding of the non-native substrate protein and GroES to the cis open ring of GroEL initiates productive folding of the non-native protein inside a highly stable GroEL-ATP-GroES complex (PubMed:9285593, PubMed:9285585, PubMed:19915138, PubMed:22445172). Binding of ATP and GroES induces conformational changes that result in the release of the substrate protein into a nano-cage compartment, within the GroEL central cavity, for folding in isolation (PubMed:8861908, PubMed:9285585, PubMed:16684774, PubMed:22445172). To discharge GroES and substrate protein, ATP hydrolysis in the cis ring is required to form a GroEL-ADP-GroES complex with decreased stability (PubMed:9285593). Finally, binding of ATP to the opposite trans ring of GroEL results in disassembly of the cis-ternary complex, which opens the cage and allows release of the folded protein (PubMed:9285593, PubMed:9285585). Proteins released in non-native form may be rapidly rebound by another GroEL complex until all of the initially bound polypeptide reaches native form (PubMed:7915201, PubMed:7867798). Can rescue kinetically trapped intermediates (PubMed:20603018). GroEL shows ATPase activity (PubMed:379350, PubMed:1676490, PubMed:9285593). ATP hydrolysis moves the reaction cycle forward but is not required for substrate folding (PubMed:9285593)., Also plays a role in coupling between replication of the F plasmid and cell division of the cell., (Microbial infection) Essential for the assembly of several bacteriophages. Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back (PubMed:1361169, PubMed:15327959, PubMed:7935790, PubMed:8846220, PubMed:9285585). Interacts with the co-chaperonin GroES (PubMed:1361169, PubMed:7638600, PubMed:7638601, PubMed:8618836, PubMed:8663256, PubMed:9285585, PubMed:25174333). Can form asymmetrical complexes, composed of one GroEL and one GroES, and symmetrical complexes, formed between one GroEL and two GroES oligomers (PubMed:1361169, PubMed:7638600, PubMed:7638601, PubMed:8618836, PubMed:8663256, PubMed:25174333). The asymmetrical complex is the functional unit (PubMed:7638600, PubMed:7638601, PubMed:25912285). It was suggested that the symmetric heterooligomer may represent a transient intermediate in the chaperonin protein folding cycle (PubMed:8618836, PubMed:8663256). Another study shows that the symmetric heterooligomers are substantially populated only in the presence of proteins that cannot be folded by the chaperonin (PubMed:25912285).

Also known as CH60_ECOLI, groEL, groL, mopA. Together with its co-chaperonin GroES, plays an essential role in assisting protein folding (PubMed:2897629, PubMed:2573517, PubMed:10532860, PubMed ...

EXTERNAL LINKS

groEL

Mutations

Mutation(s) distribution

Mutations table