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Literature summary for 3.6.4.B10 extracted from

  • Moparthi, S.B.; Carlsson, U.; Vincentelli, R.; Jonsson, B.H.; Hammarstroem, P.; Wenger, J.
    Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components (2016), Sci. Rep., 6, 28386 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.B10

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Bos taurus
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 ADP + phosphate
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 ?

Organism

Organism UniProt Comment Textmining
Bos taurus Q32L40 AND Q3ZBH0 AND Q3T0K2 AND F1N0E5 AND F1MWD3 AND Q3MHL7 AND Q2NKZ1 AND Q3ZCI9 genes CCT1-5, 6A, 7, and 8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Bos taurus ADP + phosphate
-
 ?
additional information comparison of the mechanisms of action of the GroEL/GroES and the TRiC chaperonin systems on MreB client protein variants extracted from E.scherichia coli. MreB is a homologue to actin in prokaryotes. Single-molecule fluorescence correlation spectroscopy (FCS) and time-resolved fluorescence polarization anisotropy report the binding interaction of folding MreB with GroEL, GroES and TRiC. Fluorescence resonance energy transfer (FRET) measurements on MreB variants quantifiy molecular distance changes occurring during conformational rearrangements within folding MreB bound to chaperonins Bos taurus ?
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Synonyms

Synonyms Comment Organism
CCT
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 Bos taurus
TriC
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 Bos taurus

General Information

General Information Comment Organism
evolution the protein MreB structure is rearranged by a binding-induced expansion mechanism in TRiC, GroEL and GroES. These results are quantitatively comparable to the structural rearrangements found during the interaction of beta-actin with GroEL and TRiC, indicating that the mechanism of chaperonins is conserved during evolution Bos taurus
metabolism comparison of the mechanisms of action of the GroEL/GroES and the TRiC chaperonin systems on MreB client protein variants extracted from Escherichia coli. MreB is a homologue to actin in prokaryotes Bos taurus
additional information enzyme structure homology modelling using the structure of TRiC/ADP (PDB ID 4A13, Bos taurus) and of GroES and GroEL/ES/ATP (PDB ID 1AON, Escherichia coli). Structure comparisons, overview Bos taurus
physiological function chaperonins are large, multimeric, barrel-shaped proteins, which assist in the folding and prevent aggregation of non-native proteins. The protein MreB structure is rearranged by a binding-induced expansion mechanism in TRiC, GroEL and GroES. These results are quantitatively comparable to the structural rearrangements found during the interaction of beta-actin with GroEL and TRiC. The chaperonin-bound MreB is also significantly compacted after addition of AMP-PNP for both the GroEL/ES and TRiC systems. Most importantly, GroES may act as an unfoldase by inducing a dramatic initial expansion of MreB (even more than for GroEL) implicating a role for MreB folding, suggesting a delivery mechanism for GroES to GroEL in prokaryotes Bos taurus