Any feedback?
Literature summary for 3.6.4.B10 extracted from
- Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC (2017), PLoS ONE, 12, e0176054 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| genes cct1-8, recombinant overexpression of Strep-tagged wild-type and mutant CCT complexes in Escherichia coli strain BL21 Star(DE3)pRARE | Thermochaetoides thermophila |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| recombinant enzyme, removal of all surface exposed cysteine residues for diffracted X-ray tracking experiment, and addition of cysteine residues at the tip of helical protrusions of selected two subunits. Gold nanocrystals are attached onto CtCCTs via gold-thiol bonds and applied for the analysis by diffracted X-ray tracking | Thermochaetoides thermophila |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | generation of CtCCT variants containing ATPase-deficient subunits. Removal of all surface exposed cysteine residues for diffracted X-ray tracking experiment, and addition of cysteine residues at the tip of helical protrusions of selected two subunits. Gold nanocrystals are attached onto CtCCTs via gold-thiol bonds and applied for the analysis by diffracted X-ray tracking. Irrespective of the locations of cysteines, ATP binding induces tilting motion followed by rotational motion in the CtCCT molecule, like the archaeal group II chaperonins. When gold nanocrystals are attached onto two subunits in the high ATPase activity hemisphere, the CtCCT complex exhibits a fairly rapid response to the motion. In contrast, the response of CtCCT, which has gold nanocrystals attached to the low-activity hemisphere, is slow. Change from an open to a closed state using caged-ATP, which is a derivative of ATP that is inactive and does not bind to the ATP binding site of the chaperonin | Thermochaetoides thermophila |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Thermochaetoides thermophila | 5829 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Thermochaetoides thermophila |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 950000 | - |
purified recombinant CCT complex, about, sequence calculation | Thermochaetoides thermophila |
| 970000 | - |
purified recombinant CCT complex, about, gel filtration | Thermochaetoides thermophila |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Thermochaetoides thermophila | - |
ADP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermochaetoides thermophila | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant Strep-tagged wild-type and mutant CCT complexes from Escherichia coli strain BL21 Star(DE3)pRARE by affinity and anion exchange chromatography, and gel filtration | Thermochaetoides thermophila |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | thermophilic fungus, Chaetomium thermophilum, thrives optimally at 50-55°C | Thermochaetoides thermophila | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Thermochaetoides thermophila | ADP + phosphate | - |
? | |
| additional information | ATP-dependent conformational change starts with the high-affinity hemisphere and progresses to the low-affinity hemisphere of the enzyme complex. CtCCT is immobilized on a Strep-Tactin column and acid-denatured actin and tubulin are applied to it. CtCCT is eluted by D-desthiobiotin, CtCCT binds to denatured actin and tubulin. Detailed analysis of ATP-induced conformational change in recombinant CCT using diffracted X-ray tracking, overview | Thermochaetoides thermophila | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterohexadecamer | CCT is composed of 8 different paralogous subunits, two octamers form a ring structure, a complicated structure | Thermochaetoides thermophila |
| More | CCT is composed of 8 different paralogue subunits. They are designated CCT1, CCT2, CCT3, CCT4 CCT5, CCT6, CCT7 and CCT8. They are also named CCTalpha, CCTbeta, CCTgamma, CCTdelta, CCTepsilon, CCTzeta, CCTeta, and CCTtheta. CCT subunits share a high amino acid similarity in the phosphate binding loop and the catalytic site but have a low amino acid sequence similarity in the nucleotide binding site, and they may generate variation in ATP binding and hydrolysis capability | Thermochaetoides thermophila |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CCT | - |
Thermochaetoides thermophila |
| chaperonin-containing t-complex polypeptide 1 | - |
Thermochaetoides thermophila |
| CtCCT | - |
Thermochaetoides thermophila |
| eukaryotic group II chaperonin | - |
Thermochaetoides thermophila |
| group II chaperonin CCT/TRiC | - |
Thermochaetoides thermophila |
| TCP-1 ring complex | - |
Thermochaetoides thermophila |
| TriC | - |
Thermochaetoides thermophila |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
assay at | Thermochaetoides thermophila |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | 7.5 | assay at | Thermochaetoides thermophila |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Thermochaetoides thermophila | expression of CCT is not induced by stress conditions | additional information |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | chaperonins are subdivided into two families, group I and group II chaperonins | Thermochaetoides thermophila |
| additional information | protein-folding mechanism mediated by group II chaperonins, overview. Asymmetry in the function and dynamics is shown by the cytosolic group II chaperonin CCT/TRiC. CtCCT subunits had similar characteristics in the ATP-binding pocket | Thermochaetoides thermophila |
| physiological function | the eukaryotic group II chaperonin, the chaperonin-containing t-complex polypeptide 1 (CCT), plays an important role in cytosolic proteostasis. About 10% of cytosolic proteins interact with CCT during their folding process. Expression of CCT is not induced by stress conditions, but it seems to be required for folding newly synthesized polypeptides. Despite its substrate specificity, CCT is absolutely required for folding many essential proteins, including cytoskeletal proteins such as tubulin and actin, as well as cell cycle regulators, such as CDC20 and CDH1 | Thermochaetoides thermophila |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
