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3.6.4.B10: chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)

This is an abbreviated version!
For detailed information about chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing), go to the full flat file.

Word Map on EC 3.6.4.B10

Reaction

ATP
+
H2O
=
ADP
+
phosphate

Synonyms

alpha/beta-thermosome, ApCpnB, archaeal chaperonin, CCT, CCT ATPase, CCT chaperonin, CCT complex, CCT/TRiC, CCT/TRiC chaperonin, CCT/TRiC complex, CCT2, chaperonin B, chaperonin containing t-complex polypeptide-1, chaperonin containing TCP-1, chaperonin containing TCP1, chaperonin TCP-1 ring complex, chaperonin TRiC, chaperonin TRiC/CCT, chaperonin-containing t-complex polypeptide 1, cPKA, CpkB, CtCCT, cytosolic chaperonin TRiC, eukaryotic chaperone complex, eukaryotic chaperonin, eukaryotic chaperonin TRiC, eukaryotic group II chaperonin, GaTRiC, group II chaperonin, group II chaperonin CCT/TRiC, group II CPN, HsTRiC, Mm-cpn, MmCpn, More, PfCPN, PfTRiC, PhCPN, Plasmodium TRiC, protein P45, T-complex polypeptide-1 ring complex, T-complex protein 1, T-complex protein 1 ring complex, T-complex protein-1 ring complex, TCP-1, TCP-1 ring complex, TCP1, TCP1 ring complex, thermosome, TKS1-CPN, TriC, TRiC chaperonin, TRiC chaperonin complex, TRiC/CCT, type II chaperonin

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.4 Acting on acid anhydrides to facilitate cellular and subcellular movement
                3.6.4.B10 chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)

Crystallization

Crystallization on EC 3.6.4.B10 - chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure analysis of the open conformation of the mammalian chaperonin CCT in complex with tubulin, overview
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
cryo-specimen preparation of AML-1-ETO DNA-binding domain (AML1-175), with TRiC and Hsp70, and cryo-EM imaging, three-dimensional cryo-EM map reconstruction, modelling, method, overview. TRiC can refold denatured AML1-175 (DBD) and restore its DNA binding activity in vitro. Reconstructed the TRiC-AML1-175 complex forms in the presence of Ni2+-gold nanoparticles capable of binding to the His-tag on AML1-175. Ni-affinity nanogold particles reveal the location of AML1-175 on TRiC
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
structure analysis of the open conformation of the mammalian chaperonin CCT in complex with tubulin, overview
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
crystal structure analysis, PDB ID 3KFK
crystal structure analysis, PDB IDs 3IYF and 3LOS, enzyme in open and closed state conformation
-
homology model of the FAB1 apical domain and the top scoring model was with the 2.2 A resolution mouse CCTgamma apical domain template, PDB ID 1GML
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
cryo-EM structures of Saccharomyces cerevisiae TRiC in a nucleotide partially preloaded (NPP) state and in the ATP-bound state at 4.7 A and 4.6 A resolution, respectively
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
crystal structure analysis, PDB ID 4D8Q
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
-