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Chaperonin GroEL

Together with its co-chaperonin GroES, plays an essential role in assisting protein folding^{1,2,3,4,5,6,7,8,9,10,11}. 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^{12,13,14,15,16}. 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^17,18,19,20. 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^21,22,23,24. To discharge GroES and substrate protein, ATP hydrolysis in the cis ring is required to form a GroEL-ADP-GroES complex with decreased stability²⁵. 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^26,27. Proteins released in non-native form may be rapidly rebound by another GroEL complex until all of the initially bound polypeptide reaches native form^28,29. Can rescue kinetically trapped intermediates³⁰. GroEL shows ATPase activity^31,32,33. ATP hydrolysis moves the reaction cycle forward but is not required for substrate folding³⁴. 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.

AlphaFold DB , UniProt , Accession P0A6F5, Species ECOLI (Escherichia coli (strain K12)), Gene groEL, Length 548 aa.