Protein Variants | Comment | Organism |
---|---|---|
A399T | site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 90fold | Escherichia coli |
A92T | site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 1600fold | Escherichia coli |
D115N | site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 50fold | Escherichia coli |
E191G | site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 300fold | Escherichia coli |
additional information | construction of a single-ring GroELSR. GroELSRA399T-GroES and GroELSRD115N-GroES single-ring systems support cell growth in the same manner as the wild-type double-ring GroELeGroES at 37°C and 42°C, while mutant GroELSRA92T-GroES complements GroEL-GroES at both 37°C and 42°C, and mutant GroELSRE191G-GroES complements GroEL-GroES to a lesser extent at 37°C, but not at 42°C. Activities of functional single-ring GroELSReGroES system mutants, overview | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + a folded polypeptide | - |
Escherichia coli | ADP + phosphate + an unfolded polypeptide | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GroEl | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
GroES | GroES decreases the ATP hydrolysis rate of GroEL by 50% and exerts a greater inhibitory effect on GroELSR than GroEL, as it decreases ATP hydrolysis activity of GroELSR to 5-10% of the intrinsic rate of GroELSR. Interaction analysis between the single-ring GroELSR mutants and GroES, GroES cycles between association with and dissociation off the single-ring GroELSR variants. The diminished ATPase activity of the GroELSReGroES system is due to formation of a highly stable GroELSReGroES complex with a half life t1/2 of about 300 min | Escherichia coli |