Literature summary for 3.6.4.B10 extracted from

Zang, Y.; Jin, M.; Wang, H.; Cui, Z.; Kong, L.; Liu, C.; Cong, Y.
Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM (2016), Nat. Struct. Mol. Biol., 23, 1083-1091 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Saccharomyces cerevisiae

Inhibitors

Inhibitors	Comment	Organism	Structure
AMP-PNP	ADP (or ATP, with a minor likelihood) remains bound on the CCT6 side of TRiC in the presence of excess AMP-PNP (10 mM), although some of the ADP may be replaced by AMP-PNP	Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079	genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Saccharomyces cerevisiae	ADP + phosphate	-	?
additional information	eukaryotic chaperonin TRiC (CCT) shows a staggered ATP binding mechanism, staggrered binding of ATP on the CCT6 side of nucleotide partially preloaded (NPP) stated TRiC. ATP binding affects TRiC inter- and intraring interactions. The ATP binding affinity varies among the eight distinct subunits of TRiC. Multiple modes of nucleotide binding in yeast TRiC, detailed overview. The staggered ATP binding mechanism may actually result from the delayed release of the residual ADP of these three subunits CCT8, CCT6, and CCT3	Saccharomyces cerevisiae	?	-	-

Subunits

Subunits	Comment	Organism
heterohexadecamer	dimer of octamers, analysis of subunit locations in open-state TRiC by inner-subunit eGFP tagging, overview. TRiC has a double-ring structure, and each ring consists of eight homologous but distinct subunits arranged in a specific order	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
CCT	-	Saccharomyces cerevisiae
eukaryotic chaperonin TRiC	-	Saccharomyces cerevisiae

General Information

General Information	Comment	Organism
evolution	TRiC has evolved into a complex structurally divided into two sides whose nucleotide binding and ring closure occur in a staggered manner, thus making it a highly coordixadnated macromolecular machine	Saccharomyces cerevisiae
additional information	the CCT2 subunit pair forms an unexpected Z shape. ATP binding induces a dramatic conformational change on the CCT2 side, thereby suggesting that CCT2 plays an essential role in TRiC allosteric cooperativity. The TRiC nucleotide cycle coordinates with its mechanical cycle in preparing folding intermediates for further productive folding, overview. The five ATP-binding subunits (CCT1-CCT4-CCT2-CCT5-CCT7) are located symmetrically around the on-axis CCT2 subunit in both rings and occupying one entire side of the complex. Accordingly, the ATP-driven conformational changes prixadmarily occur on that side. In contrast, the opposite CCT6 side of the complex (CCT8-CCT6-CCT3), most probably with ADP bound or partially occupying the nucleotide pocket, remains mostly poised in the ATP binding process. Thus, it appears that TRiC has evolved to be structurally divided into two sides. In addition, all of the sixteen subunits have their nucleotide pockets fully occupied in the further-refined yeast TRiC X-ray structure in the conformation with both rings tightly closed, thus suggesting that the subunits on the CCT6 side also have ATP-binding and ATP-hydrolysis abilities	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)