5VCA

VCP like ATPase from T. acidophilum (VAT)-Substrate bound conformation

5VCA の概要

• エントリーDOI: 10.2210/pdb5vca/pdb
• 関連するPDBエントリー: 5VC7
• EMDBエントリー: 8658 8659
• 分子名称: VCP-like ATPase (1 entity in total)
• 機能のキーワード: aaa+, atpase, complex, unfoldase, hydrolase
• 由来する生物種: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 377977.48

構造登録者

Ripstein, Z.A.,Huang, R.,Augustyniak, R.,Kay, L.E.,Rubinstein, J.L. (登録日: 2017-03-31, 公開日: 2017-04-26, 最終更新日: 2024-11-06)

主引用文献

Ripstein, Z.A.,Huang, R.,Augustyniak, R.,Kay, L.E.,Rubinstein, J.L.
Structure of a AAA+ unfoldase in the process of unfolding substrate.
Elife, 6:-, 2017

PubMed Abstract: AAA+ unfoldases are thought to unfold substrate through the central pore of their hexameric structures, but how this process occurs is not known. VAT, the homologue of eukaryotic CDC48/p97, works in conjunction with the proteasome to degrade misfolded or damaged proteins. We show that in the presence of ATP, VAT with its regulatory N-terminal domains removed unfolds other VAT complexes as substrate. We captured images of this transient process by electron cryomicroscopy (cryo-EM) to reveal the structure of the substrate-bound intermediate. Substrate binding breaks the six-fold symmetry of the complex, allowing five of the six VAT subunits to constrict into a tight helix that grips an ~80 Å stretch of unfolded protein. The structure suggests a processive hand-over-hand unfolding mechanism, where each VAT subunit releases the substrate in turn before re-engaging further along the target protein, thereby unfolding it.

PubMed: 28390173
DOI: 10.7554/eLife.25754

実験手法

ELECTRON MICROSCOPY (4.8 Å)