6NR9
hTRiC-hPFD Class5
Summary for 6NR9
| Entry DOI | 10.2210/pdb6nr9/pdb |
| EMDB information | 0490 0491 0492 0493 0494 0495 0496 |
| Descriptor | T-complex protein 1 subunit alpha, Prefoldin subunit 2, Prefoldin subunit 3, ... (14 entities in total) |
| Functional Keywords | tric/cct, pfd, cryoem, molecular chaperone, protein folding, chaperone |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 22 |
| Total formula weight | 981455.53 |
| Authors | Gestaut, D.,Roh, S.H.,Ma, B.,Pintilie, G.,Joachimiak, L.A.,Leitner, A.,Walzthoeni, T.,Aebersold, R.,Chiu, W.,Frydman, J. (deposition date: 2019-01-23, release date: 2019-06-19, Last modification date: 2024-03-20) |
| Primary citation | Gestaut, D.,Roh, S.H.,Ma, B.,Pintilie, G.,Joachimiak, L.A.,Leitner, A.,Walzthoeni, T.,Aebersold, R.,Chiu, W.,Frydman, J. The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis. Cell, 177:751-765.e15, 2019 Cited by PubMed Abstract: Maintaining proteostasis in eukaryotic protein folding involves cooperation of distinct chaperone systems. To understand how the essential ring-shaped chaperonin TRiC/CCT cooperates with the chaperone prefoldin/GIMc (PFD), we integrate cryoelectron microscopy (cryo-EM), crosslinking-mass-spectrometry and biochemical and cellular approaches to elucidate the structural and functional interplay between TRiC/CCT and PFD. We find these hetero-oligomeric chaperones associate in a defined architecture, through a conserved interface of electrostatic contacts that serves as a pivot point for a TRiC-PFD conformational cycle. PFD alternates between an open "latched" conformation and a closed "engaged" conformation that aligns the PFD-TRiC substrate binding chambers. PFD can act after TRiC bound its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles. Disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates. The supra-chaperone assembly formed by PFD and TRiC is essential to prevent toxic conformations and ensure effective cellular proteostasis. PubMed: 30955883DOI: 10.1016/j.cell.2019.03.012 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8.5 Å) |
Structure validation
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