5XMK

Cryo-EM structure of the ATP-bound Vps4 mutant-E233Q complex with Vta1 (masked)

5XMK の概要

• エントリーDOI: 10.2210/pdb5xmk/pdb
• EMDBエントリー: 6734
• 分子名称: Vacuolar protein sorting-associated protein 4, Vacuolar protein sorting-associated protein VTA1, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: atpase, escrtiii, vps4, vta1, protein transport
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 590806.38

構造登録者

Sun, S.,Li, L.,Yang, F.,Wang, X.,Fan, F.,Li, X.,Wang, H.,Sui, S. (登録日: 2017-05-15, 公開日: 2017-08-09, 最終更新日: 2024-03-27)

主引用文献

Sun, S.,Li, L.,Yang, F.,Wang, X.,Fan, F.,Yang, M.,Chen, C.,Li, X.,Wang, H.W.,Sui, S.F.
Cryo-EM structures of the ATP-bound Vps4(E233Q) hexamer and its complex with Vta1 at near-atomic resolution
Nat Commun, 8:16064-16064, 2017

PubMed Abstract: The cellular ESCRT-III (endosomal sorting complex required for transport-III) and Vps4 (vacuolar protein sorting 4) comprise a common machinery that mediates a variety of membrane remodelling events. Vps4 is essential for the machinery function by using the energy from ATP hydrolysis to disassemble the ESCRT-III polymer into individual proteins. Here, we report the structures of the ATP-bound Vps4 hexamer and its complex with the cofactor Vta1 (vps twenty associated 1) at resolutions of 3.9 and 4.2 Å, respectively, determined by electron cryo-microscopy. Six Vps4 subunits in both assemblies exhibit a spiral-shaped ring-like arrangement. Locating at the periphery of the hexameric ring, Vta1 dimer bridges two adjacent Vps4 subunits by two different interaction modes to promote the formation of the active Vps4 hexamer during ESCRT-III filament disassembly. The structural findings, together with the structure-guided biochemical and single-molecule analyses, provide important insights into the process of the ESCRT-III polymer disassembly by Vps4.

PubMed: 28714467
DOI: 10.1038/ncomms16064

実験手法

ELECTRON MICROSCOPY (4.18 Å)