8SFF

CCT G beta 5 complex closed state 0

8SFF の概要

• エントリーDOI: 10.2210/pdb8sff/pdb
• EMDBエントリー: 40440
• 分子名称: T-complex protein 1 subunit alpha, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (13 entities in total)
• 機能のキーワード: cct, gb5, complex, open, chaperone
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 17
• 化学式量合計: 969929.32

構造登録者

Wang, S.,Sass, M.,Willardson, B.M.,Shen, P.S. (登録日: 2023-04-11, 公開日: 2023-10-25, 最終更新日: 2023-11-15)

主引用文献

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

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

実験手法

ELECTRON MICROSCOPY (3.2 Å)