+検索条件
-Structure paper
| タイトル | Cryo-EM structures of the ATP-bound Vps4 hexamer and its complex with Vta1 at near-atomic resolution. |
|---|---|
| ジャーナル・号・ページ | Nat Commun, Vol. 8, Page 16064, Year 2017 |
| 掲載日 | 2017年7月17日 |
著者 | Shan Sun / Lin Li / Fan Yang / Xiaojing Wang / Fenghui Fan / Mengyi Yang / Chunlai Chen / Xueming Li / Hong-Wei Wang / Sen-Fang Sui / ![]() |
| PubMed 要旨 | 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. ...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. |
リンク | Nat Commun / PubMed:28714467 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.9 - 4.25 Å |
| 構造データ | EMDB-6733, PDB-5xmi: EMDB-6734, PDB-5xmk: ![]() EMDB-6735: ![]() EMDB-6736: |
| 化合物 | ![]() ChemComp-ATP: |
| 由来 |
|
キーワード | PROTEIN TRANSPORT / ATPase / EESCRTIII / Vps4 / ESCRTIII / Vta1 |
ムービー
コントローラー
構造ビューア
万見文献について



著者
リンク







キーワード