TRiC (complex)

{{short description|Multiprotein complex used in cellular proteostasis}}

File:PDB-5GW5-TRiC-AMP-PNP.png TRiC in the AMP-PNP bound state (PDB 5GW5).{{cite journal | last1=Zang | first1=Yunxiang | last2=Jin | first2=Mingliang | last3=Wang | first3=Huping | last4=Cui | first4=Zhicheng | last5=Kong | first5=Liangliang | last6=Liu | first6=Caixuan | last7=Cong | first7=Yao | title=Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM | journal=Nature Structural & Molecular Biology | publisher=Springer Science and Business Media LLC | volume=23 | issue=12 | date=2016-10-24 | issn=1545-9993 | doi=10.1038/nsmb.3309 | pages=1083–1091| pmid=27775711 | s2cid=12001964 }}]]

T-complex protein Ring Complex (TRiC), otherwise known as Chaperonin Containing TCP-1 (CCT),{{efn|The term "TCP-1" is variously expanded as "T-complex protein 1" and "tailless complex polypeptide 1". The "T-complex" is the same as tailless complex, a CCT locus associated with tail length in mice.}} is a multiprotein complex and the chaperonin of eukaryotic cells. Like the bacterial GroEL, the TRiC complex aids in the folding of ~10% of the proteome, and actin and tubulin are some of its best known substrates.{{cite journal | last1=Balchin | first1=David | last2=Hayer-Hartl | first2=Manajit | last3=Hartl | first3=F. Ulrich | title=In vivo aspects of protein folding and quality control | journal=Science | publisher=American Association for the Advancement of Science (AAAS) | volume=353 | issue=6294 | date=2016-06-30 | issn=0036-8075 | doi=10.1126/science.aac4354 | page=aac4354| pmid=27365453 | hdl=11858/00-001M-0000-002B-0856-C | s2cid=5174431 | hdl-access=free }}{{cite journal | last1=Gestaut | first1=Daniel | last2=Limatola | first2=Antonio | last3=Joachimiak | first3=Lukasz | last4=Frydman | first4=Judith | title=The ATP-powered gymnastics of TRiC/CCT: an asymmetric protein folding machine with a symmetric origin story | journal=Current Opinion in Structural Biology | publisher=Elsevier BV | volume=55 | year=2019 | issn=0959-440X | doi=10.1016/j.sbi.2019.03.002 | pages=50–58| pmid=30978594 | pmc=6776438 }} TRiC is an example of a biological machine that folds substrates within the central cavity of its barrel-like assembly using the energy from ATP hydrolysis.