8SFF
CCT G beta 5 complex closed state 0
Summary for 8SFF
| Entry DOI | 10.2210/pdb8sff/pdb |
| EMDB information | 40440 |
| Descriptor | T-complex protein 1 subunit alpha, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (13 entities in total) |
| Functional Keywords | cct, gb5, complex, open, chaperone |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 17 |
| Total formula weight | 969929.32 |
| Authors | Wang, S.,Sass, M.,Willardson, B.M.,Shen, P.S. (deposition date: 2023-04-11, release date: 2023-10-25, Last modification date: 2023-11-15) |
| Primary citation | Wang, S.,Sass, M.I.,Kwon, Y.,Ludlam, W.G.,Smith, T.M.,Carter, E.J.,Gladden, N.E.,Riggi, M.,Iwasa, J.H.,Willardson, B.M.,Shen, P.S. Visualizing the chaperone-mediated folding trajectory of the G protein beta 5 beta-propeller. Mol.Cell, 83:3852-3868.e6, 2023 Cited by PubMed Abstract: The Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with β-propeller domains. Here, we determine the structures of human CCT in complex with its accessory co-chaperone, phosducin-like protein 1 (PhLP1), in the process of folding Gβ, a component of Regulator of G protein Signaling (RGS) complexes. Cryoelectron microscopy (cryo-EM) and image processing reveal an ensemble of distinct snapshots that represent the folding trajectory of Gβ from an unfolded molten globule to a fully folded β-propeller. These structures reveal the mechanism by which CCT directs Gβ folding through initiating specific intermolecular contacts that facilitate the sequential folding of individual β sheets until the propeller closes into its native structure. This work directly visualizes chaperone-mediated protein folding and establishes that CCT orchestrates folding by stabilizing intermediates through interactions with surface residues that permit the hydrophobic core to coalesce into its folded state. PubMed: 37852256DOI: 10.1016/j.molcel.2023.09.032 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
Download full validation report
