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Literature summary for 3.6.4.B10 extracted from
- The mechanism and function of group II chaperonins (2015), J. Mol. Biol., 427, 2919-2930.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis, PDB IDs 3IYF and 3LOS, enzyme in open and closed state conformation | Methanococcus maripaludis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G160S | the TRiC-like mutant G160S of MmCpn has a drastically slower rate of ATP hydrolysis, roughly equivalent to the steady-state hydrolysis of eukaryotic TRiC | Methanococcus maripaludis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Saccharomyces cerevisiae | 5829 | - |
| cytosol | - |
Thermoplasma acidophilum | 5829 | - |
| cytosol | - |
Methanococcus maripaludis | 5829 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Saccharomyces cerevisiae |  |
| Mg2+ | required | Thermoplasma acidophilum | |
| Mg2+ | required | Methanococcus maripaludis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Saccharomyces cerevisiae | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Thermoplasma acidophilum | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Methanococcus maripaludis | - |
ADP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanococcus maripaludis | - |
- |
- |
| Saccharomyces cerevisiae | - |
- |
- |
| Thermoplasma acidophilum | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Saccharomyces cerevisiae | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Thermoplasma acidophilum | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Methanococcus maripaludis | ADP + phosphate | - |
? | |
| ATP + H2O | nucleotide binding structure and conformational changes, overview | Saccharomyces cerevisiae | ADP + phosphate | - |
? | |
| ATP + H2O | nucleotide binding structure and conformational changes, overview | Thermoplasma acidophilum | ADP + phosphate | - |
? | |
| ATP + H2O | nucleotide binding structure and conformational changes, overview | Methanococcus maripaludis | ADP + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| oligomer | subunit arrangement of the hetero-oligomeric eukaryotic chaperonin TRiC | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alpha/beta-thermosome | - |
Thermoplasma acidophilum |
| CCT | - |
Saccharomyces cerevisiae |
| MmCpn | - |
Methanococcus maripaludis |
| TriC | - |
Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the archetypal group II chaperonins. Group II chaperonins are found in archaea and the eukaryotic cytosol. They consist of two stacked rings, each composed of eight 50- to 60-kDa subunits, but do not have an obligate co-chaperone in the same manner as the group I chaperonins. Rather, they contain a built-in lid that closes the folding chamber and are thus competent to fold substrates in vitro without the assistance of accessory proteins. Group II chaperonins appear to be at the heart of a complex network of co-chaperones. The eukaryotic group II chaperonin, i.e. TRiC/CCT, differs from its simpler archaeal homologues in that it is composed of eight paralogous subunits, while in eukaryotic chaperonin, TRiC/CCT, each ring contains eight distinct, paralogous subunits occupying fixed positions in the complex | Thermoplasma acidophilum |
| evolution | the enzyme belongs to the archetypal group II chaperonins. Group II chaperonins are found in archaea and the eukaryotic cytosol. They consist of two stacked rings, each composed of eight 50- to 60-kDa subunits, but do not have an obligate co-chaperone in the same manner as the group I chaperonins. Rather, they contain a built-in lid that closes the folding chamber and are thus competent to fold substrates in vitro without the assistance of accessory proteins. Group II chaperonins appear to be at the heart of a complex network of co-chaperones. The eukaryotic group II chaperonin, i.e. TRiC/CCT, differs from its simpler archaeal homologues in that it is composed of eight paralogous subunits, while in eukaryotic chaperonin, TRiC/CCT, each ring contains eight distinct, paralogous subunits occupying fixed positions in the complex | Methanococcus maripaludis |
| evolution | the enzyme belongs to the eukaryotic group II chaperonins. Group II chaperonins are found in archaea and the eukaryotic cytosol. They consist of two stacked rings, each composed of eight 50- to 60-kDa subunits, but do not have an obligate co-chaperone in the same manner as the group I chaperonins. Rather, they contain a built-in lid that closes the folding chamber and are thus competent to fold substrates in vitro without the assistance of accessory proteins. Group II chaperonins appear to be at the heart of a complex network of co-chaperones, e.g. the phosducin-like proteins that enhance TRiC-mediated folding of several substrates. The eukaryotic group II chaperonin, i.e. TRiC/CCT, differs from its simpler archaeal homologues in that it is composed of eight paralogous subunits, while in eukaryotic chaperonin, TRiC/CCT, each ring contains eight distinct, paralogous subunits occupying fixed positions in the complex | Saccharomyces cerevisiae |
| additional information | enzyme structure and architecture comparisons and modeling, structure-function analysis of group II chaperonins, ATP-driven conformational cycle of the group II chaperonin, overview | Saccharomyces cerevisiae |
| additional information | enzyme structure and architecture comparisons and modeling, structure-function analysis of group II chaperonins, ATP-driven conformational cycle of the group II chaperonin, overview | Thermoplasma acidophilum |
| additional information | enzyme structure and architecture comparisons and modeling, structure-function analysis of group II chaperonins, ATP-driven conformational cycle of the group II chaperonin, overview | Methanococcus maripaludis |
| physiological function | the enzymes TRiC/CCT are 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. About 10% of cytosolic proteins interact with the eukaryotic chaperonin TRiC/CCT along their folding trajectory | Saccharomyces cerevisiae |
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