5UIE

Vps4-Vta1 complex

5UIE の概要

• エントリーDOI: 10.2210/pdb5uie/pdb
• EMDBエントリー: 8549 8550 8551 8552 8553 8554 8555 8556 8557
• 分子名称: Vacuolar protein sorting-associated protein 4, DOA4-independent degradation protein 4, Vacuolar protein sorting-associated protein VTA1, ... (6 entities in total)
• 機能のキーワード: vps4, escrt, vta1, aaa atpase, transport protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 19
• 化学式量合計: 740846.86

構造登録者

Monroe, N.,Shen, P.,Han, H.,Sundquist, W.I.,Hill, C.P. (登録日: 2017-01-13, 公開日: 2017-04-12, 最終更新日: 2024-11-20)

主引用文献

Monroe, N.,Han, H.,Shen, P.S.,Sundquist, W.I.,Hill, C.P.
Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase.
Elife, 6:-, 2017

PubMed Abstract: Many important cellular membrane fission reactions are driven by ESCRT pathways, which culminate in disassembly of ESCRT-III polymers by the AAA ATPase Vps4. We report a 4.3 Å resolution cryo-EM structure of the active Vps4 hexamer with its cofactor Vta1, ADP·BeF, and an ESCRT-III substrate peptide. Four Vps4 subunits form a helix whose interfaces are consistent with ATP binding, is stabilized by Vta1, and binds the substrate peptide. The fifth subunit approximately continues this helix but appears to be dissociating. The final Vps4 subunit completes a notched-washer configuration as if transitioning between the ends of the helix. We propose that ATP binding propagates growth at one end of the helix while hydrolysis promotes disassembly at the other end, so that Vps4 'walks' along ESCRT-III until it encounters the ordered N-terminal domain to destabilize the ESCRT-III lattice. This model may be generally applicable to other protein-translocating AAA ATPases.

PubMed: 28379137
DOI: 10.7554/eLife.24487

実験手法

ELECTRON MICROSCOPY (5.7 Å)