7LUP

Human TRiC/CCT complex with reovirus outer capsid protein sigma-3

Summary for 7LUP

• Entry DOI: 10.2210/pdb7lup/pdb
• EMDB information: 23522 23526
• Descriptor: T-complex protein 1 subunit epsilon, ZINC ION, T-complex protein 1 subunit beta, ... (11 entities in total)
• Functional Keywords: tric, cct, reovirus capsid, sigma 3, chaperone
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 17
• Total formula weight: 988406.70

Authors

Knowlton, J.J.,Gestaut, D.,Ma, B.,Taylor, G.,Seven, A.B.,Leitner, A.,Wilson, G.J.,Shanker, S.,Yates, N.A.,Prasad, B.V.V.,Aebersold, R.,Chiu, W.,Frydman, J.,Dermody, T.S. (deposition date: 2021-02-22, release date: 2021-03-03, Last modification date: 2024-03-06)

Primary citation

Knowlton, J.J.,Gestaut, D.,Ma, B.,Taylor, G.,Seven, A.B.,Leitner, A.,Wilson, G.J.,Shanker, S.,Yates, N.A.,Prasad, B.V.V.,Aebersold, R.,Chiu, W.,Frydman, J.,Dermody, T.S.
Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: Intracellular protein homeostasis is maintained by a network of chaperones that function to fold proteins into their native conformation. The eukaryotic TRiC chaperonin (TCP1-ring complex, also called CCT for cytosolic chaperonin containing TCP1) facilitates folding of a subset of proteins with folding constraints such as complex topologies. To better understand the mechanism of TRiC folding, we investigated the biogenesis of an obligate TRiC substrate, the reovirus σ3 capsid protein. We discovered that the σ3 protein interacts with a network of chaperones, including TRiC and prefoldin. Using a combination of cryoelectron microscopy, cross-linking mass spectrometry, and biochemical approaches, we establish functions for TRiC and prefoldin in folding σ3 and promoting its assembly into higher-order oligomers. These studies illuminate the molecular dynamics of σ3 folding and establish a biological function for TRiC in virus assembly. In addition, our findings provide structural and functional insight into the mechanism by which TRiC and prefoldin participate in the assembly of protein complexes.

PubMed: 33836586
DOI: 10.1073/pnas.2018127118

Experimental method

ELECTRON MICROSCOPY (6.2 Å)