Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.6.4.B10 extracted from

  • Balchin, D.; Milicic, G.; Strauss, M.; Hayer-Hartl, M.; Hartl, F.U.
    Pathway of actin folding directed by the eukaryotic chaperonin TRiC (2018), Cell, 174, 1507-1521.e16 .
    View publication on PubMed
Search for more literature for 3.6.4.B10

Activating Compound

Activating Compound Comment Organism Structure
prefoldin PFD, is required for protein substrate folding Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Homo sapiens
-
 ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990 genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Homo sapiens ADP + phosphate
-
 ?
additional information the hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein actin. Actin fails to fold spontaneously even in the absence of aggregation but populates a kinetically trapped, conformationally dynamic state. Analysis of the unique features of TRiC directing the folding pathway of an obligate eukaryotic substrate, overview. Binding to TRiC stabilizes a native-like structure in actin. ATP binding induces an asymmetric TRiC intermediate and selective actin release. Substrate recognition mechanism by GroEL and TRiC, and folding mechanism of actin overview Homo sapiens ?
-
-

Subunits

Subunits Comment Organism
octamer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
CCT
-
 Homo sapiens
eukaryotic chaperone complex
-
 Homo sapiens
TriC
-
 Homo sapiens

General Information

General Information Comment Organism
metabolism pathway of actin folding directed by the eukaryotic chaperonin TRiC, overview Homo sapiens
additional information conformational dynamics of native and chaperonin-bound actin by equilibrium hydrogen/deuterium exchange-mass spectrometry, overview Homo sapiens
physiological function The hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein actin. The eukaryotic chaperone complex TRiC, but not the simpler bacterial chaperonin system, GroEL/GroES, is able to induce the proper folding of actin. Actin fails to fold spontaneously, strictly requiring TRiC chaperonin for folding. Actin binding to TRiC specifies a unique topology for productive folding. ATP binding induces an asymmetric TRiC intermediate and selective actin release. Stepwise folding on and inside TRiC allows actin to access the native state Homo sapiens