Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + a folded polypeptide | folding of the model substrate HippelLindau tumor suppressor protein VHL in an ATP-dependent manner. Heterogeneity of the action of GroES/EL on a bound polypeptide substrate might arise from the random nature of the specific binding to the various identical subunits of GroEL, and might help explain why multiple rounds of binding and hydrolysis are required for some chaperonin substrates | Escherichia coli | ADP + phosphate + an unfolded polypeptide | - |
? |
Synonyms | Comment | Organism |
---|---|---|
chaperonin GroEL/ES | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
GroES | cofactor. ATP- and GroES-induced confinement within the GroEL cavity remodels bound polypeptides by causing expansion (or racking) of some regions and compaction of others, most notably, the hydrophobic core | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | the double ring-shaped chaperonin GroEL binds a wide range of non-native polypeptides within its central cavity and, together with its cofactor GroES, assists their folding in an ATP-dependent manner | Escherichia coli |