7RUC

Metazoan pre-targeting GET complex with SGTA (cBUGGS)

7RUC の概要

• エントリーDOI: 10.2210/pdb7ruc/pdb
• EMDBエントリー: 24700 24701 24702
• 分子名称: ATPase GET3, Golgi to ER traffic protein 4 homolog, Large proline-rich protein BAG6, ... (7 entities in total)
• 機能のキーワード: atpase, complex, membrane protein chaperone, chaperone
• 由来する生物種: Danio rerio (Zebrafish, Brachydanio rerio); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 200364.63

構造登録者

Keszei, A.F.A.,Yip, M.C.J.,Shao, S. (登録日: 2021-08-16, 公開日: 2021-12-15, 最終更新日: 2024-06-05)

主引用文献

Keszei, A.F.A.,Yip, M.C.J.,Hsieh, T.C.,Shao, S.
Structural insights into metazoan pretargeting GET complexes.
Nat.Struct.Mol.Biol., 28:1029-1037, 2021

PubMed Abstract: Close coordination between chaperones is essential for protein biosynthesis, including the delivery of tail-anchored (TA) proteins containing a single C-terminal transmembrane domain to the endoplasmic reticulum (ER) by the conserved GET pathway. For successful targeting, nascent TA proteins must be promptly chaperoned and loaded onto the cytosolic ATPase Get3 through a transfer reaction involving the chaperone SGTA and bridging factors Get4, Ubl4a and Bag6. Here, we report cryo-electron microscopy structures of metazoan pretargeting GET complexes at 3.3-3.6 Å. The structures reveal that Get3 helix 8 and the Get4 C terminus form a composite lid over the Get3 substrate-binding chamber that is opened by SGTA. Another interaction with Get4 prevents formation of Get3 helix 4, which links the substrate chamber and ATPase domain. Both interactions facilitate TA protein transfer from SGTA to Get3. Our findings show how the pretargeting complex primes Get3 for coordinated client loading and ER targeting.

PubMed: 34887561
DOI: 10.1038/s41594-021-00690-7

実験手法

ELECTRON MICROSCOPY (3.6 Å)