7YLX

yeast TRiC-plp2-actin complex at S4 closed TRiC state

Summary for 7YLX

• Entry DOI: 10.2210/pdb7ylx/pdb
• EMDB information: 33920
• Descriptor: T-complex protein 1 subunit alpha, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (13 entities in total)
• Functional Keywords: tric/cct, actin, phosducin-like protein, chaperone
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 17
• Total formula weight: 1010175.48

Authors

Han, W.Y. (deposition date: 2022-07-27, release date: 2023-03-29, Last modification date: 2024-07-03)

Primary citation

Han, W.,Jin, M.,Liu, C.,Zhao, Q.,Wang, S.,Wang, Y.,Yin, Y.,Peng, C.,Wang, Y.,Cong, Y.
Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.
Sci Adv, 9:eade1207-eade1207, 2023

PubMed Abstract: The cytoskeletal proteins tubulin and actin are the obligate substrates of TCP-1 ring complex/Chaperonin containing TCP-1 (TRiC/CCT), and their folding involves co-chaperone. Through cryo-electron microscopy analysis, we present a more complete picture of TRiC-assisted tubulin/actin folding along TRiC adenosine triphosphatase cycle, under the coordination of co-chaperone plp2. In the open S1/S2 states, plp2 and tubulin/actin engaged within opposite TRiC chambers. Notably, we captured an unprecedented TRiC-plp2-tubulin complex in the closed S3 state, engaged with a folded full-length -tubulin and loaded with a guanosine triphosphate, and a plp2 occupying opposite rings. Another closed S4 state revealed an actin in the intermediate folding state and a plp2. Accompanying TRiC ring closure, plp2 translocation could coordinate substrate translocation on the CCT6 hemisphere, facilitating substrate stabilization and folding. Our findings reveal the folding mechanism of the major cytoskeletal proteins tubulin/actin under the coordination of the biogenesis machinery TRiC and plp2 and extend our understanding of the links between cytoskeletal proteostasis and related human diseases.

PubMed: 36921056
DOI: 10.1126/sciadv.ade1207

Experimental method

ELECTRON MICROSCOPY (3.2 Å)