Organism | UniProt | Comment | Textmining |
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Escherichia coli | - |
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- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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additional information | GroEL binds only one molecule of the model substrate Rubisco. In contrast, the capsid protein of bacteriophage T4, a natural GroEL substrate, can occupy both rings simultaneously. Each substrate induces distinct conformational changes in the GroEL chaperonin. Binding of Rubisco to the GroEL oligomer stabilizes the chaperonin complex significantly, whereas binding of one capsid protein does not have the same effect. Addition of a second capsid protein molecule to GroEL results in a similar stabilizing effect to that obtained after the binding of a single Rubisco. The binding of a single capsid polypeptide does not induce significant conformational changes in the GroEL trans ring, and hence the unoccupied GroEL ring remains accessible for a second capsid molecule | Escherichia coli | ? | - |
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Synonyms | Comment | Organism |
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GroEL chaperonin | - |
Escherichia coli |