7NVL

Human TRiC complex in closed state with nanobody bound (Consensus Map)

7NVL の概要

• エントリーDOI: 10.2210/pdb7nvl/pdb
• EMDBエントリー: 12605
• 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: tric, cct, atp hydrolysis, type ii chaperonin, protein folding, structural genomics, structural genomics consortium, sgc, chaperone
• 由来する生物種: Lama glama; 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 984566.53

構造登録者

Kelly, J.J.,Chi, G.,Bulawa, C.,Paavilainen, V.O.,Bountra, C.,Huiskonen, J.T.,Yue, W.,Structural Genomics Consortium (SGC) (登録日: 2021-03-15, 公開日: 2022-03-02, 最終更新日: 2024-11-13)

主引用文献

Kelly, J.J.,Tranter, D.,Pardon, E.,Chi, G.,Kramer, H.,Happonen, L.,Knee, K.M.,Janz, J.M.,Steyaert, J.,Bulawa, C.,Paavilainen, V.O.,Huiskonen, J.T.,Yue, W.W.
Snapshots of actin and tubulin folding inside the TRiC chaperonin.
Nat.Struct.Mol.Biol., 29:420-429, 2022

PubMed Abstract: The integrity of a cell's proteome depends on correct folding of polypeptides by chaperonins. The chaperonin TCP-1 ring complex (TRiC) acts as obligate folder for >10% of cytosolic proteins, including he cytoskeletal proteins actin and tubulin. Although its architecture and how it recognizes folding substrates are emerging from structural studies, the subsequent fate of substrates inside the TRiC chamber is not defined. We trapped endogenous human TRiC with substrates (actin, tubulin) and cochaperone (PhLP2A) at different folding stages, for structure determination by cryo-EM. The already-folded regions of client proteins are anchored at the chamber wall, positioning unstructured regions toward the central space to achieve their native fold. Substrates engage with different sections of the chamber during the folding cycle, coupled to TRiC open-and-close transitions. Further, the cochaperone PhLP2A modulates folding, acting as a molecular strut between substrate and TRiC chamber. Our structural snapshots piece together an emerging model of client protein folding within TRiC.

PubMed: 35449234
DOI: 10.1038/s41594-022-00755-1

実験手法

ELECTRON MICROSCOPY (2.5 Å)