Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged wild-type and mutant enzyme oligomer rings in Escherichia coli | Thermococcus sp. |
Protein Variants | Comment | Organism |
---|---|---|
K165A/K485W | site-directed mutagenesis, ATPase inactive mutant that can partially prevent the spontaneous refolding ofGFP and refold it in an ATP-dependent manner | Thermococcus sp. |
K485W | site-directed mutagenesis, the mutant shows ATP binding and conformational change upon ATP binding | Thermococcus sp. |
additional information | construction of the asymmetric ring complex of a group II chaperonin using circular permutated covalent mutants, TKS1-CPNASR. Although one ring of the asymmetric ring complex lacks ATPase or ATP binding activity, the other wild-type ring undergoes an ATP-dependent conformational change and maintains protein-folding activity. It is possible to construct covalent chaperonin complexes by connecting N and C-termini. Circular permutated covalent enzyme TKS1-CPN (CPNCPC) is constructed by applying circular permutation to the covalent TKS1-CPN dimer, the circular permutated covalent TKS1-CPN dimer that has the deletion of 95 amino acids from its N-terminus and the addition of the same 95 amino acids to its C-terminus can assemble into a doublering structure similar to the wild-type. The 95th amino acid residue is located at the loop region between Helix 4 and Helix 5. The complex of the TKS1-CPN variant has ann molecular weight of approximately 120 kDa determined by SDS-PAGE. The ATPase activity of mutant CPNASR is half that of the recombinant His-tagged CPNwild-type homooligomer. Phenotypes, overview | Thermococcus sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Thermococcus sp. | - |
ADP + phosphate | - |
? | |
ATP + H2O | Thermococcus sp. KS-1 | - |
ADP + phosphate | - |
? | |
ATP + H2O | Thermococcus sp. KS1 | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus sp. | O24730 | beta-subunit | - |
Thermococcus sp. | P61112 | alpha-subunit | - |
Thermococcus sp. KS-1 | O24730 | beta-subunit | - |
Thermococcus sp. KS1 | P61112 | alpha-subunit | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type and mutant enzyme oligomer rings from Escherichia coli | Thermococcus sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Thermococcus sp. | ADP + phosphate | - |
? | |
ATP + H2O | - |
Thermococcus sp. KS-1 | ADP + phosphate | - |
? | |
ATP + H2O | - |
Thermococcus sp. KS1 | ADP + phosphate | - |
? | |
additional information | enzyme TKS1-CPN shows a strong protein-folding activity | Thermococcus sp. | ? | - |
? | |
additional information | enzyme TKS1-CPN shows a strong protein-folding activity | Thermococcus sp. KS-1 | ? | - |
? | |
additional information | enzyme TKS1-CPN shows a strong protein-folding activity | Thermococcus sp. KS1 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
TKS1-CPN | - |
Thermococcus sp. |
General Information | Comment | Organism |
---|---|---|
additional information | chaperonins are ubiquitous molecular chaperones with the subunit molecular mass of 60 kDa. They exist as double-ring oligomers with central cavities. An ATP-dependent conformational change of the cavity induces the folding of an unfolded protein that is captured in the cavity. Inter-ring communication is dispensable in the reaction cycle of group II chaperonins. Group II chaperonins do not require a co-chaperonin but have a built-in lid that is composed of a helical protrusion in the apical domain. The built-in lid seals off the central cavity and induces a conformational change to assist the folding of the trapped substrate, molecular mechanism analysis. Structure modeling of wild-type and mutant enzyme oligomers using structure of Thermococcus sp. JCM 11816, PDB ID 1Q2V, overview | Thermococcus sp. |
physiological function | chaperonins are ubiquitous molecular chaperones performing an ATP-dependent conformational change of the cavity that induces the folding of an unfolded protein that is captured in the cavity | Thermococcus sp. |