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Literature summary for 3.6.4.B10 extracted from
- Dynamics, flexibility, and allostery in molecular chaperonins (2015), FEBS Lett., 589, 2522-2532.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis, PDB ID 3KFK | Methanococcus maripaludis |
| crystal structure analysis, PDB ID 4D8Q | Saccharomyces cerevisiae |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Thermoplasma acidophilum | 5829 | - |
| cytosol | - |
Methanococcus maripaludis | 5829 | - |
| cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
| cytosol | - |
Bos taurus | 5829 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Methanococcus maripaludis |  |
| Mg2+ | required | Saccharomyces cerevisiae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Methanococcus maripaludis | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Saccharomyces cerevisiae | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Saccharomyces cerevisiae ATCC 204508 | - |
ADP + phosphate | - |
? | |
| additional information | Saccharomyces cerevisiae | TRiC mediates protein folding by encapsulation. It utilizes a built-in lid mechanism of helical protrusions extending from the apical domains that function similar to the blades of a camera iris. This mechanism allows linker sequences between sequential protein domains to protrude through the narrow oculus of the aperture for domain-wise protein encapsulation. The apical domains of the paralogous subunits differ in their specificity for substrate protein binding, allowing TRiC to mediate the folding of a range of structurally diverse proteins including tubulins and actin, as well as many proteins with WD40 beta-propeller domains. Cavity closure is triggered by ATP hydrolysis, not ATP binding. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation | ? | - |
? | |
| additional information | Saccharomyces cerevisiae ATCC 204508 | TRiC mediates protein folding by encapsulation. It utilizes a built-in lid mechanism of helical protrusions extending from the apical domains that function similar to the blades of a camera iris. This mechanism allows linker sequences between sequential protein domains to protrude through the narrow oculus of the aperture for domain-wise protein encapsulation. The apical domains of the paralogous subunits differ in their specificity for substrate protein binding, allowing TRiC to mediate the folding of a range of structurally diverse proteins including tubulins and actin, as well as many proteins with WD40 beta-propeller domains. Cavity closure is triggered by ATP hydrolysis, not ATP binding. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | Q32L40 | alpha-subunit | - |
| Methanococcus maripaludis | Q877G8 | - |
- |
| Saccharomyces cerevisiae | P12612 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 | P12612 | - |
- |
| Thermoplasma acidophilum | P48424 | alpha-subunit | - |
| Thermoplasma acidophilum | P48425 | beta-subunit | - |
| Thermoplasma acidophilum ATCC 25905 | P48424 | alpha-subunit | - |
| Thermoplasma acidophilum ATCC 25905 | P48425 | beta-subunit | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Methanococcus maripaludis | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Saccharomyces cerevisiae | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | ADP + phosphate | - |
? | |
| additional information | TRiC mediates protein folding by encapsulation. It utilizes a built-in lid mechanism of helical protrusions extending from the apical domains that function similar to the blades of a camera iris. This mechanism allows linker sequences between sequential protein domains to protrude through the narrow oculus of the aperture for domain-wise protein encapsulation. The apical domains of the paralogous subunits differ in their specificity for substrate protein binding, allowing TRiC to mediate the folding of a range of structurally diverse proteins including tubulins and actin, as well as many proteins with WD40 beta-propeller domains. Cavity closure is triggered by ATP hydrolysis, not ATP binding. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | TRiC mediates protein folding by encapsulation. It utilizes a built-in lid mechanism of helical protrusions extending from the apical domains that function similar to the blades of a camera iris. This mechanism allows linker sequences between sequential protein domains to protrude through the narrow oculus of the aperture for domain-wise protein encapsulation. The apical domains of the paralogous subunits differ in their specificity for substrate protein binding, allowing TRiC to mediate the folding of a range of structurally diverse proteins including tubulins and actin, as well as many proteins with WD40 beta-propeller domains. Cavity closure is triggered by ATP hydrolysis, not ATP binding. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation | Saccharomyces cerevisiae ATCC 204508 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homooligomer | - |
Methanococcus maripaludis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CCT | - |
Bos taurus |
| chaperonin containing TCP-1 | - |
Bos taurus |
| TCP1 ring complex | - |
Bos taurus |
| thermosome | - |
Thermoplasma acidophilum |
| thermosome | - |
Methanococcus maripaludis |
| TriC | - |
Saccharomyces cerevisiae |
| TriC | - |
Bos taurus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the chaperonins of group II in the cytosol of archaea and eukaryotic cells share the three-domain subunit topology and cylindrical architecture with the group I chaperonins, EC 3.6.4.9, but function without a GroES-like cofactor | Methanococcus maripaludis |
| evolution | the chaperonins of group II in the cytosol of archaea and eukaryotic cells share the three-domain subunit topology and cylindrical architecture with the group I chaperonins, EC 3.6.4.9, but function without a GroES-like cofactor | Saccharomyces cerevisiae |
| evolution | the enzyme belongs to the group II chaperonins, group II consists of the archaeal (thermosomes) and eukaryotic cytosolic variants (CCT or TRiC). The structure is more complex for group II chaperonins compared to group I chaperonins, EC 3.6.4.9. Evolution of group II chaperonins via rapid multiple gene duplication, folding mechanism, phylogenetic analyses | Thermoplasma acidophilum |
| evolution | the enzyme belongs to the group II chaperonins, group II consists of the archaeal (thermosomes) and eukaryotic cytosolic variants (CCT or TRiC). The structure is more complex for group II chaperonins compared to group I chaperonins, EC 3.6.4.9. Evolution of group II chaperonins via rapid multiple gene duplication, folding mechanism, phylogenetic analyses | Bos taurus |
| additional information | group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation CCT (chaperonin containing TCP1) or TRiC (TCP1 ring complex) is composed of eight distinct subunits (CCTalpha-1, CCTbeta-2, CCTgamma-3, CCTdelta-4, CCTepsilon-5, CCTzeta-6, CCTeta-7 and CCTtheta-8) organized in a unique intra- and inter-ring arrangement, structure modeling, detailed overview. The substrate-binding region in each of the subunits bears charged and hydrophilic residues in some subunits, whereas other subunits have hydrophobic residues | Bos taurus |
| additional information | group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation, structure modeling, detailed overview | Thermoplasma acidophilum |
| additional information | group II chaperonins generally contain eight subunits per ring and have a tendency to heterooligomer formation. TRiC contains eight paralogous subunits per ring assembled in a defined order | Methanococcus maripaludis |
| additional information | group II chaperonins generally contain eight subunits per ring and have a tendency to heterooligomer formation. TRiC contains eight paralogous subunits per ring assembled in a defined order | Saccharomyces cerevisiae |
| additional information | mechanisms and the structure-function relationships in the complex protein systems, structural dynamics, allostery, and associated conformational rearrangements, overview. Group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation, structure modeling, detailed overview | Thermoplasma acidophilum |
| physiological function | chaperonins are essential for protein folding in all domains of life. They stand out among ATP-dependent chaperones in that they form large 800-1000 kDa double-ring complexes with an internal chamber in each ring. Their basic function is to provide a nano-cage for the folding of single protein molecules to occur in isolation, unimpaired by aggregation | Methanococcus maripaludis |
| physiological function | chaperonins are essential for protein folding in all domains of life. They stand out among ATP-dependent chaperones in that they form large 800-1000 kDa double-ring complexes with an internal chamber in each ring. Their basic function is to provide a nano-cage for the folding of single protein molecules to occur in isolation, unimpaired by aggregation. Enzyme TRiC mediates protein folding by encapsulation and displays negative inter-ring cooperativity, favoring asymmetric complexes with one ring open and the other closed. The inner surface of the TRiC chamber is divided into two halves with opposite charge character. This charge asymmetry coincides with an asymmetry in ATP binding and hydrolysis: four adjacent subunits have high affinity for ATP and neutral or negative surface charge, while the other four subunits have low affinity for ATP and positive surface charge. Chamber closure and release of substrate protein can initiate asymmetrically and proceed in a sequential mechanism. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation | Saccharomyces cerevisiae |
| physiological function | chaperonins have elaborate allosteric mechanisms to regulate their functional cycle. Long-range negative cooperativity between the two rings ensures alternation of the folding chambers. No Positive intra-ring cooperativity in group II enzymes | Bos taurus |
| physiological function | chaperonins have elaborate allosteric mechanisms to regulate their functional cycle. Long-range negative cooperativity between the two rings ensures alternation of the folding chambers. No Positive intra-ring cooperativity in group II enzymes. Thermosomes use a non-specific, hydrophobic-based substrate recognition mechanism involving the helical protrusion, release of trapped substrate after closure of the chaperonin cavity | Thermoplasma acidophilum |
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