8UB4

Cdc48-Shp1 unfolding native substrate, consensus structure

8UB4 の概要

• エントリーDOI: 10.2210/pdb8ub4/pdb
• EMDBエントリー: 42076
• 分子名称: Cell division control protein 48, Substrate, UBX domain-containing protein 1, ... (6 entities in total)
• 機能のキーワード: unfoldase, aaa atpase, p97, chaperone, cdc48
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 700445.19

構造登録者

Cooney, I.,Schubert, H.L.,Cedeno, K.,Carson, R.,Fisher, O.N.,Price, J.C.,Hill, C.P.,Shen, P.S. (登録日: 2023-09-22, 公開日: 2024-11-06, 最終更新日: 2025-05-28)

主引用文献

Cooney, I.,Schubert, H.L.,Cedeno, K.,Fisher, O.N.,Carson, R.,Price, J.C.,Hill, C.P.,Shen, P.S.
Visualization of the Cdc48 AAA+ ATPase protein unfolding pathway.
Nat Commun, 15:7505-7505, 2024

PubMed Abstract: The Cdc48 AAA+ ATPase is an abundant and essential enzyme that unfolds substrates in multiple protein quality control pathways. The enzyme includes two conserved AAA+ ATPase motor domains, D1 and D2, that assemble as hexameric rings with D1 stacked above D2. Here, we report an ensemble of native structures of Cdc48 affinity purified from budding yeast lysate in complex with the adaptor Shp1 in the act of unfolding substrate. Our analysis reveals a continuum of structural snapshots that spans the entire translocation cycle. These data uncover elements of Shp1-Cdc48 interactions and support a 'hand-over-hand' mechanism in which the sequential movement of individual subunits is closely coordinated. D1 hydrolyzes ATP and disengages from substrate prior to D2, while D2 rebinds ATP and re-engages with substrate prior to D1, thereby explaining the dominant role played by the D2 motor in substrate translocation/unfolding.

PubMed: 39209885
DOI: 10.1038/s41467-024-51835-3

実験手法

ELECTRON MICROSCOPY (2.9 Å)