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Literature summary extracted from

  • Skjaerven, L.; Cuellar, J.; Martinez, A.; Valpuesta, J.M.
    Dynamics, flexibility, and allostery in molecular chaperonins (2015), FEBS Lett., 589, 2522-2532.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.4.B10 crystal structure analysis, PDB ID 3KFK Methanococcus maripaludis
3.6.4.B10 crystal structure analysis, PDB ID 4D8Q Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.4.B10 cytosol
-
 Thermoplasma acidophilum 5829
-
3.6.4.B10 cytosol
-
 Methanococcus maripaludis 5829
-
3.6.4.B10 cytosol
-
 Saccharomyces cerevisiae 5829
-
3.6.4.B10 cytosol
-
 Bos taurus 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.4.B10 Mg2+ required Methanococcus maripaludis
3.6.4.B10 Mg2+ required Saccharomyces cerevisiae
5.6.1.7 Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.4.B10 ATP + H2O Methanococcus maripaludis
-
 ADP + phosphate
-
 ?
3.6.4.B10 ATP + H2O Saccharomyces cerevisiae
-
 ADP + phosphate
-
 ?
3.6.4.B10 ATP + H2O Saccharomyces cerevisiae ATCC 204508
-
 ADP + phosphate
-
 ?
3.6.4.B10 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 ?
-
 ?
3.6.4.B10 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 ?
-
 ?
5.6.1.7 ATP + H2O + a folded polypeptide Escherichia coli
-
 ADP + phosphate + an unfolded polypeptide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.B10 Bos taurus Q32L40 alpha-subunit
-
3.6.4.B10 Methanococcus maripaludis Q877G8
-
-
3.6.4.B10 Saccharomyces cerevisiae P12612
-
-
3.6.4.B10 Saccharomyces cerevisiae ATCC 204508 P12612
-
-
3.6.4.B10 Thermoplasma acidophilum P48424 alpha-subunit
-
3.6.4.B10 Thermoplasma acidophilum P48425 beta-subunit
-
3.6.4.B10 Thermoplasma acidophilum ATCC 25905 P48424 alpha-subunit
-
3.6.4.B10 Thermoplasma acidophilum ATCC 25905 P48425 beta-subunit
-
5.6.1.7 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.B10 ATP + H2O
-
 Methanococcus maripaludis ADP + phosphate
-
 ?
3.6.4.B10 ATP + H2O
-
 Saccharomyces cerevisiae ADP + phosphate
-
 ?
3.6.4.B10 ATP + H2O
-
 Saccharomyces cerevisiae ATCC 204508 ADP + phosphate
-
 ?
3.6.4.B10 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 ?
-
 ?
3.6.4.B10 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 ?
-
 ?
5.6.1.7 ATP + H2O + a folded polypeptide
-
 Escherichia coli ADP + phosphate + an unfolded polypeptide
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.4.B10 homooligomer
-
 Methanococcus maripaludis

Synonyms

EC Number Synonyms Comment Organism
3.6.4.B10 CCT
-
 Bos taurus
3.6.4.B10 chaperonin containing TCP-1
-
 Bos taurus
3.6.4.B10 TCP1 ring complex
-
 Bos taurus
3.6.4.B10 thermosome
-
 Thermoplasma acidophilum
3.6.4.B10 thermosome
-
 Methanococcus maripaludis
3.6.4.B10 TriC
-
 Saccharomyces cerevisiae
3.6.4.B10 TriC
-
 Bos taurus
5.6.1.7 GroEl
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
3.6.4.B10 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
3.6.4.B10 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
3.6.4.B10 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
3.6.4.B10 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
3.6.4.B10 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
3.6.4.B10 additional information group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation, structure modeling, detailed overview Thermoplasma acidophilum
3.6.4.B10 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
3.6.4.B10 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
3.6.4.B10 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
3.6.4.B10 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
3.6.4.B10 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
3.6.4.B10 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
3.6.4.B10 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
5.6.1.7 evolution the chaperonins are a family of molecular chaperones present in all three kingdoms of life. They are classified into group I and group II. Group I consists of the bacterial variants (GroEL) and the eukaryotic ones from mitochondria and chloroplasts (Hsp60). Both groups assemble into a dual ring structure, with each ring providing a protective folding chamber for nascent and denatured proteins Escherichia coli
5.6.1.7 additional information mechanisms and the structure-function relationships in the complex protein systems, structural dynamics, allostery, and associated conformational rearrangements, overview Escherichia coli
5.6.1.7 physiological function the chaperonin functional cycle is powered by ATP binding and hydrolysis, which drives a series of structural rearrangements that enable encapsulation and subsequent release of the substrate protein. Chaperonins have elaborate allosteric mechanisms to regulate their functional cycle. Long-range negative cooperativity between the two rings ensures alternation of the folding chambers. Positive intra-ring cooperativity, which facilitates concerted conformational transitions within the protein subunits of one ring, has only been demonstrated for group I chaperonins Escherichia coli