Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8SGL

CCT G beta 5 complex closed state 15

Summary for 8SGL
Entry DOI10.2210/pdb8sgl/pdb
EMDB information40461
DescriptorT-complex protein 1 subunit alpha, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (13 entities in total)
Functional Keywordscct, gb5, complex, open, chaperone
Biological sourceHomo sapiens (human)
More
Total number of polymer chains17
Total formula weight979226.09
Authors
Wang, S.,Sass, M.,Willardson, B.M.,Shen, P.S. (deposition date: 2023-04-12, release date: 2023-10-25, Last modification date: 2023-11-15)
Primary citationWang, 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: 37852256
DOI: 10.1016/j.molcel.2023.09.032
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon